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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
A0008201molecular_functionheparin binding
A0010466biological_processnegative regulation of peptidase activity
A0030193biological_processregulation of blood coagulation
B0004867molecular_functionserine-type endopeptidase inhibitor activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0007596biological_processblood coagulation
B0008201molecular_functionheparin binding
B0010466biological_processnegative regulation of peptidase activity
B0030193biological_processregulation of blood coagulation
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: BINDING => ECO:0000250
ChainResidueDetails
ALEU82
AILE162
AGLY178
BLEU82
BILE162
BGLY178

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Reactive bond
ChainResidueDetails
AARG426
BARG426

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01008
ChainResidueDetails
ATYR64
BTYR64

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01008
ChainResidueDetails
AASP69
BASP69

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
ACYS129
AGLY168
AASN188
ALEU225
BCYS129
BGLY168
BASN188
BLEU225

224201

PDB entries from 2024-08-28

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