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3DGV

Crystal structure of thrombin activatable fibrinolysis inhibitor (TAFI)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004181molecular_functionmetallocarboxypeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008270molecular_functionzinc ion binding
A0042730biological_processfibrinolysis
B0004181molecular_functionmetallocarboxypeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008270molecular_functionzinc ion binding
B0042730biological_processfibrinolysis
C0004181molecular_functionmetallocarboxypeptidase activity
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0008270molecular_functionzinc ion binding
C0042730biological_processfibrinolysis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues182
DetailsPropeptide: {"description":"Activation peptide","featureId":"PRO_0000282869"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues594
DetailsDomain: {"description":"Peptidase M14","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00730","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18669641","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Cleavage; by thrombin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues11
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18669641","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG127
AGLU270

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG127
BGLU270

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
CARG127
CGLU270

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
AARG71
AGLU270
AARG127

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
BARG71
BGLU270
BARG127

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cbx
ChainResidueDetails
CARG71
CGLU270
CARG127

253795

PDB entries from 2026-05-20

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