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1X7A

Porcine Factor IXa Complexed to 1-{3-[amino(imino)methyl]phenyl}-N-[4-(1H-benzimidazol-1-yl)-2-fluorophenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide

Functional Information from GO Data
ChainGOidnamespacecontents
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
L0005509molecular_functioncalcium ion binding
L0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 187 C 298
ChainResidue
CASN97
CILE213
CSER214
CTRP215
CGLY216
CGLU217
CGLU219
CCYS220
CGLY226
CTYR99
CARG143
CPHE174
CASP189
CSER190
CCYS191
CGLN192
CSER195

Functional Information from PROSITE/UniProt
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCqvGFegkn....C
ChainResidueDetails
LCYS71-CYS82
LCYS109-CYS124

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
CVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
ChainResidueDetails
CASP189-VAL200

site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
LCYS62-CYS73

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EciEEkCsfeearEvfentektne.FW
ChainResidueDetails
LGLU17-TRP42

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCqvGfeGKnC
ChainResidueDetails
LCYS71-CYS82

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCepnp..........Clnggl..CkDdinsYeC
ChainResidueDetails
LASP47-CYS71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: via 4-carboxyglutamate => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LSER3
LGLY4
LGLU7
LASN13
LGLU17

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LSER24
CILE213
LPHE25
LGLU27
LPHE41
LTRP42
CVAL203
CGLY205
CPHE208
CTHR210

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by factor XIa => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LSER123
CARG150

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: 4-carboxyglutamate => ECO:0000250|UniProtKB:P00741, ECO:0000255|PROSITE-ProRule:PRU00463
ChainResidueDetails
LSER3
LGLY4
LGLU7
LVAL10
LASN13
LGLU17

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LPHE41
CTHR129

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LTYR45
LSER136

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Sulfotyrosine => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LGLY133

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; alternate => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LVAL137

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) threonine; alternate => ECO:0000250|UniProtKB:P00740
ChainResidueDetails
LVAL137

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CTRP141
CTYR228

218853

PDB entries from 2024-04-24

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