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1WQV

Human Factor Viia-Tissue Factor Complexed with propylsulfonamide-D-Thr-Met-p-aminobenzamidine

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
L0005509molecular_functioncalcium ion binding
L0005576cellular_componentextracellular region
T0007596biological_processblood coagulation
T0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC
ChainResidueDetails
LCYS61-CYS72

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW
ChainResidueDetails
LCGU16-TRP41

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfClpAfeGRnC
ChainResidueDetails
LCYS70-CYS81

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
HVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA
ChainResidueDetails
HASP189-ALA200

site_idPS00621
Number of Residues18
DetailsTISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE
ChainResidueDetails
TTRP45-GLU62

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CrCheGYslladgvsC
ChainResidueDetails
LCYS112-CYS127

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC
ChainResidueDetails
LASP46-CYS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
TASN124
TASN137
HSER195

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
HASP189

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725
ChainResidueDetails
HASN175
LCGU7
LCGU14
LCGU16
LCGU20
LCGU25
LCGU26
LCGU29
LCGU35

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:3264725
ChainResidueDetails
LCGU19

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725
ChainResidueDetails
LASP63

site_idSWS_FT_FI6
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
LSER52

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546
ChainResidueDetails
LSER60

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725
ChainResidueDetails
LASN145

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY193

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

229380

PDB entries from 2024-12-25

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