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5FPT

Structure of hepatitis C virus (HCV) full-length NS3 complex with small-molecule ligand 2-(1-methyl-1H-indol-3-yl)acetic acid (AT3437) in an alternate binding site.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processtransformation of host cell by virus
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0019087biological_processtransformation of host cell by virus
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 3VY A 1721
ChainResidue
ATHR254
AGLY255
ATHR269
AGLY271
ALYS272
ATYR502
AHOH2138

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 3VY B 1721
ChainResidue
BGLY255
BTHR269
BALA275
BTYR502
BHOH2181
BVAL232
BTHR254

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916
ChainResidueDetails
AHIS57
AASP81
BHIS57
BASP81

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
ChainResidueDetails
ASER139
BSER139

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
ChainResidueDetails
ACYS97
ACYS99
BCYS97
BCYS99

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916
ChainResidueDetails
ACYS145
AHIS149
BCYS145
BHIS149

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
AALA204
BALA204

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9WMX2
ChainResidueDetails
ASER211
AGLU291
BSER211
BGLU291

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Cleavage; by serine protease/helicase NS3 => ECO:0000250|UniProtKB:P27958
ChainResidueDetails
ATHR631
BTHR631

218853

PDB entries from 2024-04-24

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