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3OSL

Structure of bovine thrombin-activatable fibrinolysis inhibitor in complex with tick carboxypeptidase inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0004181molecular_functionmetallocarboxypeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0008233molecular_functionpeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0042730biological_processfibrinolysis
A0046872molecular_functionmetal ion binding
B0004857molecular_functionenzyme inhibitor activity
B0005576cellular_componentextracellular region
B0007596biological_processblood coagulation
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0035821biological_processmodulation of process of another organism
B0044002biological_processacquisition of nutrients from host
B0090729molecular_functiontoxin activity
C0004180molecular_functioncarboxypeptidase activity
C0004181molecular_functionmetallocarboxypeptidase activity
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0006508biological_processproteolysis
C0007596biological_processblood coagulation
C0007599biological_processhemostasis
C0008233molecular_functionpeptidase activity
C0008237molecular_functionmetallopeptidase activity
C0008270molecular_functionzinc ion binding
C0016787molecular_functionhydrolase activity
C0042730biological_processfibrinolysis
C0046872molecular_functionmetal ion binding
D0004857molecular_functionenzyme inhibitor activity
D0005576cellular_componentextracellular region
D0007596biological_processblood coagulation
D0008191molecular_functionmetalloendopeptidase inhibitor activity
D0010951biological_processnegative regulation of endopeptidase activity
D0030414molecular_functionpeptidase inhibitor activity
D0035821biological_processmodulation of process of another organism
D0044002biological_processacquisition of nutrients from host
D0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS181
AGLU184
AHIS310
BLEU74

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 999
ChainResidue
CHIS181
CGLU184
CHIS310
DLEU74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18669641","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Cleavage; by thrombin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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