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8QQ6

CRYSTAL STRUCTURE OF FVIIA IN COMPLEX WITH A BENZAMIDINE-BASED INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0007596biological_processblood coagulation
C0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC
ChainResidueDetails
ACYS61-CYS72

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW
ChainResidueDetails
ACGU16-TRP41

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfClpAfeGRnC
ChainResidueDetails
ACYS70-CYS81

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA
ChainResidueDetails
BASP189-ALA200

site_idPS00621
Number of Residues18
DetailsTISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE
ChainResidueDetails
CTRP45-GLU62

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CrCheGYslladgvsC
ChainResidueDetails
ACYS112-CYS127

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC
ChainResidueDetails
AASP46-CYS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN124
CASN137
BSER195

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP189
ACGU7
ACGU14
ACGU16
ACGU20
ACGU25
ACGU26
ACGU29
ACGU35

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725
ChainResidueDetails
BASN175

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725
ChainResidueDetails
AASP63

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201
ChainResidueDetails
ASER52

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546
ChainResidueDetails
ASER60

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PDB entries from 2025-06-11

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