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1BTH

STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
J0004252molecular_functionserine-type endopeptidase activity
J0005576cellular_componentextracellular region
J0006508biological_processproteolysis
J0007596biological_processblood coagulation
K0004252molecular_functionserine-type endopeptidase activity
K0005509molecular_functioncalcium ion binding
K0006508biological_processproteolysis
K0007596biological_processblood coagulation
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
P0004867molecular_functionserine-type endopeptidase inhibitor activity
Q0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPFV
ChainResidueDetails
HASP189-VAL200

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC
ChainResidueDetails
PPHE33-CYS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues100
DetailsDomain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Reactive bond for trypsin"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KGLY193
KHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KHIS57
KGLY196

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
KASP102
KSER195
KHIS57

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PDB entries from 2025-10-15

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