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1ATT

CRYSTAL STRUCTURE OF CLEAVED BOVINE ANTITHROMBIN III AT 3.2 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0008201molecular_functionheparin binding
A0030193biological_processregulation of blood coagulation
A0030414molecular_functionpeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0007596biological_processblood coagulation
B0007599biological_processhemostasis
B0008201molecular_functionheparin binding
B0030193biological_processregulation of blood coagulation
B0030414molecular_functionpeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FKANRPFLVlI
ChainResidueDetails
APHE403-ILE413

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Reactive bond"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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