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2WPH

factor IXa superactive triple mutant

Functional Information from GO Data
ChainGOidnamespacecontents
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA S 1246
ChainResidue
SGLU70
SASN72
SGLU75
SGLU77
SGLU80
SHOH2088

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1PE S 1247
ChainResidue
SHOH2327
SHOH2402
SHOH2404
SHOH2405
SHOH2406
SHOH2407
SHOH2408
EHOH2040
SGLU186
SARG188

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 1PE S 1248
ChainResidue
STHR76
SHIS78
SPRO90
SHIS92
SLYS148
SHOH2130
SHOH2138
SHOH2205
SHOH2410
SHOH2411
SHOH2412
SHOH2413

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
SVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
ChainResidueDetails
SASP189-VAL200

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CsCteGYrlaenqksC
ChainResidueDetails
ECYS109-CYS124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613
ChainResidueDetails
SHIS57
SSER195

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:659613
ChainResidueDetails
SASP102

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
ChainResidueDetails
SGLU70
SASN72
SGLU75
SGLU77

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
ChainResidueDetails
SGLU80

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SASP102
SSER195
SHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SASP102
SSER195
SHIS57
SGLY196

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SASP102
SSER195
SGLY193
SHIS57

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SASP102
SHIS57

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SSER195
SGLY193

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
SSER195
SGLY196

222415

PDB entries from 2024-07-10

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