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3BEF

Crystal structure of thrombin bound to the extracellular fragment of PAR1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
D0004252molecular_functionserine-type endopeptidase activity
D0005576cellular_componentextracellular region
D0006508biological_processproteolysis
D0007596biological_processblood coagulation
E0004252molecular_functionserine-type endopeptidase activity
E0005509molecular_functioncalcium ion binding
E0006508biological_processproteolysis
E0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by CTSG => ECO:0000269|PubMed:7744748
ChainResidueDetails
CPHE55
FPHE55
BSER195
EHIS57
EASN102
ESER195

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
BASN60
EASN60

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BHIS57
BGLY184

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASN102
ESER195
EHIS57

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASN102
BSER195
BGLY193
BHIS57

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASN102
ESER195
EGLY193
EHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EHIS57
EGLY184

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASN102
BHIS57

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASN102
EHIS57

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY193

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY193

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY196

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY196

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASN102
BSER195
BHIS57

237735

PDB entries from 2025-06-18

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