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5VOJ

Crystal structure of HCV NS3/4A protease in complex with JZ01-15, an analogue of 5172-mcP1P3

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processtransformation of host cell by virus
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue 9H4 A 1201
ChainResidue
AGLN1041
ALEU1135
ALYS1136
AGLY1137
ASER1138
ASER1139
APHE1154
AARG1155
AALA1156
AALA1157
ASO41202
ATHR1042
AHOH1365
AHOH1369
AHOH1382
AHOH1396
APHE1043
ATYR1056
AHIS1057
AGLY1058
AVAL1078
AASP1081
AARG1123

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 1202
ChainResidue
ATYR1006
AGLN1008
ATYR1056
A9H41201
AHOH1301
AHOH1333
AHOH1349
AHOH1360
AHOH1386

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1203
ChainResidue
ACYS1097
ACYS1099
ACYS1145
AHIS1149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
AHIS1057
AASP1081
ASER1139

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
ACYS1097
ACYS1099
ACYS1145
AHIS1149

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030
ChainResidueDetails
AASP1003

222926

PDB entries from 2024-07-24

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