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2O8M

Crystal structure of the S139A mutant of Hepatitis C Virus NS3/4A protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processtransformation of host cell by virus
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0019087biological_processtransformation of host cell by virus
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 201
ChainResidue
ACYS97
ACYS99
ACYS145
AHOH1116

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 201
ChainResidue
BCYS97
BCYS99
BCYS145
BHOH292

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA C 1001
ChainResidue
AHOH1022
CLEU231
CGLY233
CHOH1002
ATHR4

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1002
ChainResidue
AALA5
AALA111
AHOH1008
AHOH1024
BHOH246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
ChainResidueDetails
AHIS57
BHIS57

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917
ChainResidueDetails
AASP81
BASP81

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
ChainResidueDetails
AALA139
BALA139

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
ChainResidueDetails
ACYS97
ACYS99
BCYS97
BCYS99

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
ChainResidueDetails
ACYS145
BCYS145

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982
ChainResidueDetails
AHIS149
BHIS149

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 776
ChainResidueDetails
AHIS57proton shuttle (general acid/base)
AASP81electrostatic stabiliser
AGLY137electrostatic stabiliser
AALA139covalently attached, electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 776
ChainResidueDetails
BHIS57proton shuttle (general acid/base)
BASP81electrostatic stabiliser
BGLY137electrostatic stabiliser
BALA139covalently attached, electrostatic stabiliser

217705

PDB entries from 2024-03-27

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