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UniProtKB/Swiss-Prot entry P00734

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name THRB_HUMAN
Primary accession number P00734
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 128)
Name and origin of the protein
Protein name Prothrombin [Precursor]
Synonyms EC 3.4.21.5
Coagulation factor II
Contains Activation peptide fragment 1
Activation peptide fragment 2
Thrombin light chain
Thrombin heavy chain
Gene name
Name: F2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1021/bi00393a033; PubMed=2825773 [NCBI, ExPASy, EBI, Israel, Japan]
Degen S.J.F., Davie E.W.;
"Nucleotide sequence of the gene for human prothrombin.";
Biochemistry 26:6165-6177(1987).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-165.
SeattleSNPs program for genomic applications;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [MRNA] OF 8-622.
DOI=10.1021/bi00278a008; PubMed=6305407 [NCBI, ExPASy, EBI, Israel, Japan]
Degen S.J.F., McGillivray R.T.A., Davie E.W.;
"Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin.";
Biochemistry 22:2087-2097(1983).
[4]
 PROTEIN SEQUENCE OF 44-314.
PubMed=266717 [NCBI, ExPASy, EBI, Israel, Japan]
Walz D.A., Hewett-Emmett D., Seegers W.H.;
"Amino acid sequence of human prothrombin fragments 1 and 2.";
Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977).
[5]
 PROTEIN SEQUENCE OF 315-622.
PubMed=873923 [NCBI, ExPASy, EBI, Israel, Japan]
Butkowski R.J., Elion J., Downing M.R., Mann K.G.;
"Primary structure of human prethrombin 2 and alpha-thrombin.";
J. Biol. Chem. 252:4942-4957(1977).
[6]
 PROTEOLYTIC PROCESSING.
PubMed=3759958 [NCBI, ExPASy, EBI, Israel, Japan]
Rabiet M.J., Blashill A., Furie B., Furie B.C.;
"Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma.";
J. Biol. Chem. 261:13210-13215(1986).
[7]
 FUNCTION, AND CHARACTERIZATION.
PubMed=2856554 [NCBI, ExPASy, EBI, Israel, Japan]
Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.;
"Synthetic peptides bind to high-affinity thrombin receptors and modulate thrombin mitogenesis.";
Pept. Res. 1:65-73(1988).
[8]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.";
Proteomics 4:454-465(2004).
[9]
 CHARACTERIZATION OF THE TP508 PEPTIDE.
DOI=10.1016/j.orthres.2004.12.005; PubMed=15885491 [NCBI, ExPASy, EBI, Israel, Japan]
Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.;
"rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce chemotaxis of human osteoblasts and microvascular endothelial cells.";
J. Orthop. Res. 23:680-685(2005).
[10]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=2583108 [NCBI, ExPASy, EBI, Israel, Japan]
Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.;
"The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.";
EMBO J. 8:3467-3475(1989).
[12]
 X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
PubMed=2369893 [NCBI, ExPASy, EBI, Israel, Japan]
Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W., Hofsteenge J., Stone S.R.;
"Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition.";
EMBO J. 9:2361-2365(1990).
[13]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
PubMed=2374926 [NCBI, ExPASy, EBI, Israel, Japan]
Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C., Fenton J.W. II;
"The structure of a complex of recombinant hirudin and human alpha-thrombin.";
Science 249:277-280(1990).
[14]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN AND SYNTHETIC INHIBITOR.
PubMed=8251938 [NCBI, ExPASy, EBI, Israel, Japan]
Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.;
"Changes in interactions in complexes of hirudin derivatives and human alpha-thrombin due to different crystal forms.";
Protein Sci. 2:1630-1642(1993).
[15]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8071320 [NCBI, ExPASy, EBI, Israel, Japan]
Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D., Correa P.E., Fenton J.W. II, Tulinsky A.;
"Crystallographic structure of human gamma-thrombin.";
J. Biol. Chem. 269:22000-22006(1994).
[16]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1093/emboj/16.11.2977; PubMed=9214615 [NCBI, ExPASy, EBI, Israel, Japan]
van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R., Esmon C.T., Stubbs M.T.;
"The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin.";
EMBO J. 16:2977-2984(1997).
[17]
 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
DOI=10.1073/pnas.96.5.1852; PubMed=10051558 [NCBI, ExPASy, EBI, Israel, Japan]
Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E.;
"Unexpected crucial role of residue 225 in serine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999).
[18]
 X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
DOI=10.1006/jmbi.2001.4872; PubMed=11493008 [NCBI, ExPASy, EBI, Israel, Japan]
Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F., Hudson H.R., Kakkar V.V., Deadman J.J.;
"Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate.";
J. Mol. Biol. 311:549-555(2001).
[19]
 X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN AND SYNTHETIC INHIBITOR.
DOI=10.1039/b602585d; PubMed=16763681 [NCBI, ExPASy, EBI, Israel, Japan]
Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.;
"Multipolar interactions in the D pocket of thrombin: large differences between tricyclic imide and lactam inhibitors.";
Org. Biomol. Chem. 4:2364-2375(2006).
[20]
 X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN.
DOI=10.1021/ja0735002; PubMed=17685615 [NCBI, ExPASy, EBI, Israel, Japan]
Liu C.C., Brustad E., Liu W., Schultz P.G.;
"Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin.";
J. Am. Chem. Soc. 129:10648-10649(2007).
[21]
 X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC INHIBITOR.
DOI=10.1016/j.bmcl.2008.01.098; PubMed=18291642 [NCBI, ExPASy, EBI, Israel, Japan]
Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M., McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y., Lynch J.J., Lyle E.A.;
"Structure-based design of novel groups for use in the P1 position of thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.";
Bioorg. Med. Chem. Lett. 18:2062-2066(2008).
[22]
 X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5 AND HEPARIN.
DOI=10.1073/pnas.0711055105; PubMed=18362344 [NCBI, ExPASy, EBI, Israel, Japan]
Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.;
"Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
[23]
 VARIANT DYSPROTHROMBINEMIA CYS-314.
PubMed=3771562 [NCBI, ExPASy, EBI, Israel, Japan]
Rabiet M.-J., Furie B.C., Furie B.;
"Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273.";
J. Biol. Chem. 261:15045-15048(1986).
[24]
 VARIANT DYSPROTHROMBINEMIA ALA-509.
PubMed=7792730 [NCBI, ExPASy, EBI, Israel, Japan]
Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I.;
"Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala.";
Thromb. Haemost. 73:203-209(1995).
[25]
 VARIANTS DYSPROTHROMBINEMIA THR-380 AND HIS-431.
PubMed=1421398 [NCBI, ExPASy, EBI, Israel, Japan]
Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T., Yamaguchi K.;
"Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His).";
Blood 80:2275-2280(1992).
[26]
 VARIANT DYSPROTHROMBINEMIA HIS-314.
PubMed=7865694 [NCBI, ExPASy, EBI, Israel, Japan]
James H.L., Kim D.J., Zheng D.-Q., Girolami A.;
"Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site.";
Blood Coagul. Fibrinolysis 5:841-844(1994).
[27]
 VARIANT DYSPROTHROMBINEMIA CYS-425.
DOI=10.1021/bi00426a013; PubMed=3242619 [NCBI, ExPASy, EBI, Israel, Japan]
Henriksen R.A., Mann K.G.;
"Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382.";
Biochemistry 27:9160-9165(1988).
[28]
 VARIANT DYSPROTHROMBINEMIA VAL-601.
DOI=10.1021/bi00431a017; PubMed=2719946 [NCBI, ExPASy, EBI, Israel, Japan]
Henriksen R.A., Mann K.G.;
"Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity.";
Biochemistry 28:2078-2082(1989).
[29]
 VARIANT DYSPROTHROMBINEMIA ALA-509.
DOI=10.1021/bi00148a005; PubMed=1354985 [NCBI, ExPASy, EBI, Israel, Japan]
Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C., Iwanaga S.;
"Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity.";
Biochemistry 31:7457-7462(1992).
[30]
 VARIANT DYSPROTHROMBINEMIA TRP-461.
DOI=10.1021/bi00378a020; PubMed=3567158 [NCBI, ExPASy, EBI, Israel, Japan]
Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A., Iwanaga S.;
"Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima.";
Biochemistry 26:1117-1122(1987).
[31]
 VARIANT DYSPROTHROMBINEMIA TRP-461.
PubMed=3801671 [NCBI, ExPASy, EBI, Israel, Japan]
Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S., Miyoshi K., Morita T., Iwanaga S.;
"Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin.";
Blood 69:565-569(1987).
[32]
 VARIANT DYSPROTHROMBINEMIA TRP-461.
PubMed=1349838 [NCBI, ExPASy, EBI, Israel, Japan]
Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S., Itakura M.;
"Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia.";
Int. J. Hematol. 55:93-100(1992).
[33]
 VARIANT DYSPROTHROMBINEMIA LYS-200.
PubMed=6405779 [NCBI, ExPASy, EBI, Israel, Japan]
Board P.G., Shaw D.C.;
"Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site.";
Br. J. Haematol. 54:245-254(1983).
[34]
 VARIANTS MET-165 AND THR-386.
DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan]
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions of human genes.";
Nat. Genet. 22:231-238(1999).
[35]
 ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.;
Nat. Genet. 23:373-373(1999).
[36]
 INVOLVEMENT IN SUSCEPTIBILITY TO ISCHEMIC STROKE.
DOI=10.1001/archneur.61.11.1652; PubMed=15534175 [NCBI, ExPASy, EBI, Israel, Japan]
Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls.";
Arch. Neurol. 61:1652-1661(2004).
[37]
 THERAPEUTIC USAGE OF THE TP508 PEPTIDE.
DOI=10.1111/j.1524-475X.2006.00181.x; PubMed=17244316 [NCBI, ExPASy, EBI, Israel, Japan]
Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A., Zwernemann A., Ryaby J.T., Carney D.H.;
"Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a placebo-controlled phase I/II study.";
Wound Repair Regen. 15:23-34(2007).
Comments
  • FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.
  • CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
  • INTERACTION:
    Q846V4:- (xeno); NbExp=3; IntAct=EBI-297094, EBI-989571;
    P07204:THBD; NbExp=1; IntAct=EBI-297094, EBI-941422;
  • SUBCELLULAR LOCATION: Secreted, extracellular space.
  • TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
  • PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.
  • DISEASE: Defects in F2 are the cause of various forms of dysprothrombinemia [MIM:176930].
  • DISEASE: Genetic variations in F2 may be a cause of susceptibility to ischemic stroke [MIM:601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
  • PHARMACEUTICAL: The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.
  • MISCELLANEOUS: Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.
  • MISCELLANEOUS: It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting.
  • MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.
  • MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does not occur in plasma.
  • SIMILARITY: Belongs to the peptidase S1 family [view classification].
  • SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
  • SIMILARITY: Contains 2 kringle domains.
  • SIMILARITY: Contains 1 peptidase S1 domain [view classification].
  • WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry; URL="http://en.wikipedia.org/wiki/Thrombin";.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=F2";.
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f2/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M17262; AAC63054.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF478696; AAL77436.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V00595; CAA23842.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29351; TBHU.
RefSeq NP_000497.1; -.
UniGene Hs.655207
3D structure databases
PDB
1A2C; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A3B; X-ray; 1.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A3E; X-ray; 1.85 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A46; X-ray; 2.12 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A4W; X-ray; 1.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A5G; X-ray; 2.06 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1A61; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1ABI; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1ABJ; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AD8; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AE8; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AFE; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AHT; X-ray; 1.60 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AI8; X-ray; 1.85 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AIX; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AWF; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1AWH; X-ray; 3.00 A; A/C=328-363, B/D=364-622.[ExPASy / RCSB / EBI]
1AY6; X-ray; 1.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1B5G; X-ray; 2.07 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1B7X; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1BA8; X-ray; 1.80 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1BB0; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1BCU; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1BHX; X-ray; 2.30 A; A=331-360, B=364-510, F=518-622.[ExPASy / RCSB / EBI]
1BMM; X-ray; 2.60 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1BMN; X-ray; 2.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1BTH; X-ray; 2.30 A; H/K=364-622, J/L=328-363.[ExPASy / RCSB / EBI]
1C1U; X-ray; 1.75 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1C1V; X-ray; 1.98 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1C1W; X-ray; 1.90 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1C4U; X-ray; 2.10 A; 1=328-363, 2=364-622.[ExPASy / RCSB / EBI]
1C4V; X-ray; 2.10 A; 1=328-363, 2=364-622.[ExPASy / RCSB / EBI]
1C4Y; X-ray; 2.70 A; 1=328-363, 2=364-622.[ExPASy / RCSB / EBI]
1C5L; X-ray; 1.47 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1C5N; X-ray; 1.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1C5O; X-ray; 1.90 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1CA8; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1D3D; X-ray; 2.04 A; A=333-360, B=364-620.[ExPASy / RCSB / EBI]
1D3P; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1D3Q; X-ray; 2.90 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1D3T; X-ray; 3.00 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1D4P; X-ray; 2.07 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1D6W; X-ray; 2.00 A; A=334-620.[ExPASy / RCSB / EBI]
1D9I; X-ray; 2.30 A; A=334-621.[ExPASy / RCSB / EBI]
1DE7; X-ray; 2.00 A; H/K=364-622, J/L=328-363.[ExPASy / RCSB / EBI]
1DIT; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1DM4; X-ray; 2.50 A; A=328-362, B=363-622.[ExPASy / RCSB / EBI]
1DOJ; X-ray; 1.70 A; A=328-622.[ExPASy / RCSB / EBI]
1DWB; X-ray; 3.16 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1DWC; X-ray; 3.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1DWD; X-ray; 3.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1DWE; X-ray; 3.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1DX5; X-ray; 2.30 A; A/B/C/D=328-363, M/N/O/P=364-622.[ExPASy / RCSB / EBI]
1E0F; X-ray; 3.10 A; A/B/C=328-363, D/E/F=364-622.[ExPASy / RCSB / EBI]
1EB1; X-ray; 1.80 A; H=364-620, L=335-360.[ExPASy / RCSB / EBI]
1EOJ; X-ray; 2.10 A; A=332-620.[ExPASy / RCSB / EBI]
1EOL; X-ray; 2.10 A; A=332-620.[ExPASy / RCSB / EBI]
1FPC; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1FPH; X-ray; 2.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1G30; X-ray; 2.00 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1G32; X-ray; 1.90 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1G37; X-ray; 2.00 A; A=334-620.[ExPASy / RCSB / EBI]
1GHV; X-ray; 1.85 A; H=364-620, L=328-363.[ExPASy / RCSB / EBI]
1GHW; X-ray; 1.75 A; H=364-620, L=328-363.[ExPASy / RCSB / EBI]
1GHX; X-ray; 1.65 A; H=364-620, L=328-363.[ExPASy / RCSB / EBI]
1GHY; X-ray; 1.85 A; H=364-620, L=328-363.[ExPASy / RCSB / EBI]
1GJ4; X-ray; 1.81 A; H=364-621, L=328-363.[ExPASy / RCSB / EBI]
1GJ5; X-ray; 1.73 A; H=364-621, L=328-363.[ExPASy / RCSB / EBI]
1H8D; X-ray; 1.40 A; H=364-621, L=333-360.[ExPASy / RCSB / EBI]
1H8I; X-ray; 1.75 A; H=364-622, L=334-360.[ExPASy / RCSB / EBI]
1HAG; X-ray; 2.00 A; E=328-622.[ExPASy / RCSB / EBI]
1HAH; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HAI; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HAO; X-ray; 2.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HAP; X-ray; 2.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HBT; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HDT; X-ray; 2.60 A; H=364-622, L=331-363.[ExPASy / RCSB / EBI]
1HGT; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HLT; X-ray; 3.00 A; H/K=364-622, J/L=334-360.[ExPASy / RCSB / EBI]
1HUT; X-ray; 2.90 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HXE; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1HXF; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1IHS; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1IHT; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1JMO; X-ray; 2.20 A; H=363-622, L=315-362.[ExPASy / RCSB / EBI]
1JOU; X-ray; 1.80 A; A/C/E=315-363, B/D/F=364-622.[ExPASy / RCSB / EBI]
1JWT; X-ray; 2.50 A; A=328-622.[ExPASy / RCSB / EBI]
1K21; X-ray; 1.86 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1K22; X-ray; 1.93 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1KTS; X-ray; 2.40 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1KTT; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1LHC; X-ray; 1.95 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1LHD; X-ray; 2.35 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1LHE; X-ray; 2.25 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1LHF; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1LHG; X-ray; 2.25 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1MH0; X-ray; 2.80 A; A/B=334-620.[ExPASy / RCSB / EBI]
1MU6; X-ray; 1.99 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1MU8; X-ray; 2.00 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1MUE; X-ray; 2.00 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1NM6; X-ray; 1.80 A; A=335-621.[ExPASy / RCSB / EBI]
1NO9; X-ray; 1.90 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRN; X-ray; 3.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRO; X-ray; 3.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRP; X-ray; 3.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRQ; X-ray; 3.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRR; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NRS; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1NT1; X-ray; 2.00 A; A=335-621.[ExPASy / RCSB / EBI]
1NU7; X-ray; 2.20 A; A/E=332-359, B/F=364-622.[ExPASy / RCSB / EBI]
1NU9; X-ray; 2.20 A; A/D=332-622.[ExPASy / RCSB / EBI]
1NY2; X-ray; 2.30 A; 1=328-363, 2=364-622.[ExPASy / RCSB / EBI]
1NZQ; X-ray; 2.18 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1O0D; X-ray; 2.44 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1O2G; X-ray; 1.58 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1O5G; X-ray; 1.75 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1OOK; X-ray; 2.30 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1OYT; X-ray; 1.67 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1P8V; X-ray; 2.60 A; B=333-361, C=364-622.[ExPASy / RCSB / EBI]
1PPB; X-ray; 1.92 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1QBV; X-ray; 1.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1QHR; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1QJ1; X-ray; 2.00 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1QJ6; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1QJ7; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1QUR; X-ray; 2.00 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1RD3; X-ray; 2.50 A; A/C=328-363, B/D=364-622.[ExPASy / RCSB / EBI]
1RIW; X-ray; 2.04 A; A=328-363, B=364-510, C=518-622.[ExPASy / RCSB / EBI]
1SB1; X-ray; 1.90 A; H=364-621, L=333-361.[ExPASy / RCSB / EBI]
1SFQ; X-ray; 1.91 A; A/D=328-363, B/E=364-622.[ExPASy / RCSB / EBI]
1SG8; X-ray; 2.30 A; A/D=328-363, B/E=364-622.[ExPASy / RCSB / EBI]
1SGI; X-ray; 2.30 A; A/D=328-363, B/E=364-622.[ExPASy / RCSB / EBI]
1SHH; X-ray; 1.55 A; A/D=328-363, B/E=364-622.[ExPASy / RCSB / EBI]
1SL3; X-ray; 1.81 A; A=335-621.[ExPASy / RCSB / EBI]
1SR5; X-ray; 3.10 A; B=328-363, C=364-622.[ExPASy / RCSB / EBI]
1T4U; X-ray; 2.00 A; H=364-622, L=334-359.[ExPASy / RCSB / EBI]
1T4V; X-ray; 2.00 A; H=364-622, L=334-359.[ExPASy / RCSB / EBI]
1TA2; X-ray; 2.30 A; A=335-621.[ExPASy / RCSB / EBI]
1TA6; X-ray; 1.90 A; A=335-621.[ExPASy / RCSB / EBI]
1TB6; X-ray; 2.50 A; H=364-622, L=315-363.[ExPASy / RCSB / EBI]
1TBZ; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1THP; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1THR; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1THS; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1TMB; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1TMT; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1TMU; X-ray; 2.50 A; H=364-622, L=333-360.[ExPASy / RCSB / EBI]
1TOM; X-ray; 1.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1TQ0; X-ray; 2.80 A; A/C=333-363, B/D=364-620.[ExPASy / RCSB / EBI]
1TQ7; X-ray; 2.40 A; A=320-363, B=364-620.[ExPASy / RCSB / EBI]
1TWX; X-ray; 2.40 A; A=334-361, B=364-622.[ExPASy / RCSB / EBI]
1UMA; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1UVS; X-ray; 2.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1VR1; X-ray; 1.90 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1VZQ; X-ray; 1.54 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1W7G; X-ray; 1.65 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
1WAY; X-ray; 2.02 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1WBG; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
1XM1; X-ray; 2.30 A; A=328-622.[ExPASy / RCSB / EBI]
1XMN; X-ray; 1.85 A; A/C/E/G=328-363, B/D/F/H=364-622.[ExPASy / RCSB / EBI]
1YPE; X-ray; 1.81 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1YPG; X-ray; 1.80 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1YPJ; X-ray; 1.78 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1YPK; X-ray; 1.78 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1YPL; X-ray; 1.85 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1YPM; X-ray; 1.85 A; H=364-620, L=334-360.[ExPASy / RCSB / EBI]
1Z71; X-ray; 1.80 A; A=335-621.[ExPASy / RCSB / EBI]
1Z8I; X-ray; 2.00 A; A=324-361, B=364-622.[ExPASy / RCSB / EBI]
1Z8J; X-ray; 2.00 A; A=322-361, B=364-622.[ExPASy / RCSB / EBI]
1ZGI; X-ray; 2.20 A; A=335-621.[ExPASy / RCSB / EBI]
1ZGV; X-ray; 2.20 A; A=335-621.[ExPASy / RCSB / EBI]
1ZRB; X-ray; 1.90 A; A=335-621.[ExPASy / RCSB / EBI]
2A0Q; X-ray; 1.90 A; A/C=334-363, B/D=364-620.[ExPASy / RCSB / EBI]
2A2X; X-ray; 2.44 A; H=364-622, L=330-363.[ExPASy / RCSB / EBI]
2A45; X-ray; 3.65 A; A/D=328-363, B/E=364-622.[ExPASy / RCSB / EBI]
2AFQ; X-ray; 1.93 A; A/C=332-360, B/D=364-622.[ExPASy / RCSB / EBI]
2ANK; X-ray; 2.46 A; H=364-622, L=330-363.[ExPASy / RCSB / EBI]
2ANM; X-ray; 2.40 A; H=364-620, L=328-363.[ExPASy / RCSB / EBI]
2B5T; X-ray; 2.10 A; A/C=315-363, B/D=364-622.[ExPASy / RCSB / EBI]
2BDY; X-ray; 1.61 A; A=334-622.[ExPASy / RCSB / EBI]
2BVR; X-ray; 1.25 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2BVS; X-ray; 1.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2BVX; X-ray; 3.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2BXT; X-ray; 1.83 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2BXU; X-ray; 2.80 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2C8W; X-ray; 1.96 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2C8X; X-ray; 2.17 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2C8Y; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2C8Z; X-ray; 2.14 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2C90; X-ray; 2.25 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2C93; X-ray; 2.20 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2CF8; X-ray; 1.30 A; H=364-620, L=334-361.[ExPASy / RCSB / EBI]
2CF9; X-ray; 1.79 A; H=364-620, L=334-361.[ExPASy / RCSB / EBI]
2CN0; X-ray; 1.30 A; H=364-620, L=334-361.[ExPASy / RCSB / EBI]
2FEQ; X-ray; 2.44 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2FES; X-ray; 2.42 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2GDE; X-ray; 2.00 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2GP9; X-ray; 1.87 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2H9T; X-ray; 2.40 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2HGT; X-ray; 2.20 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2HNT; X-ray; 2.50 A; C=364-433, E=437-517, F=518-622, L=328-363.[ExPASy / RCSB / EBI]
2HPP; X-ray; 3.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
2HPQ; X-ray; 3.30 A; H=364-622, L=328-363, P=213-291.[ExPASy / RCSB / EBI]
2HWL; X-ray; 2.40 A; A/C=328-363, B/D=364-622.[ExPASy / RCSB / EBI]
2JH0; X-ray; 1.70 A; C=328-363, D=364-622.[ExPASy / RCSB / EBI]
2JH5; X-ray; 2.50 A; C=328-363, D=364-622.[ExPASy / RCSB / EBI]
2JH6; X-ray; 2.21 A; C=328-363, D=364-622.[ExPASy / RCSB / EBI]
2OD3; X-ray; 1.75 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2PGB; X-ray; 1.54 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2PGQ; X-ray; 1.80 A; A=319-363, B=364-622.[ExPASy / RCSB / EBI]
2PKS; X-ray; 2.50 A; A=334-360, B=364-510, C=518-619.[ExPASy / RCSB / EBI]
2PW8; X-ray; 1.84 A; H=364-621, L=334-360.[ExPASy / RCSB / EBI]
2THF; X-ray; 2.10 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2UUF; X-ray; 1.26 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2UUJ; X-ray; 1.32 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
2UUK; X-ray; 1.39 A; A=328-363, B=364-622.[ExPASy / RCSB / EBI]
3B9F; X-ray; 1.60 A; H=364-622, L=315-363.[ExPASy / RCSB / EBI]
3BEF; X-ray; 2.20 A; A/D=318-363, B/E=364-622.[ExPASy / RCSB / EBI]
3BEI; X-ray; 1.55 A; A=320-363, B=364-622.[ExPASy / RCSB / EBI]
3BF6; X-ray; 2.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
3BIU; X-ray; 2.30 A; H=364-620, L=333-361.[ExPASy / RCSB / EBI]
3BIV; X-ray; 1.80 A; H=364-620, L=333-361.[ExPASy / RCSB / EBI]
3C1K; X-ray; 1.84 A; A=335-621.[ExPASy / RCSB / EBI]
3HAT; X-ray; 2.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
3HTC; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
4HTC; X-ray; 2.30 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
4THN; X-ray; 2.50 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
5GDS; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EBI]
7KME; X-ray; 2.10 A; H=364-622, L=328-363.[ExPASy / RCSB / EB