Structure of PDB 3su4 Chain A

Receptor sequence
>3su4A (length=192) [Search protein sequence]
GSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGEVQIVSTA
TQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDLVGWQAPQ
GSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSA
GGPLLCPAGHAVGIFKAAVSTRGVAKAVDFIPVESLETTMRS
3D structure
PDB3su4 The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors.
ChainA
Resolution2.255 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H1057 D1081 G1137 A1139
Catalytic site (residue number reindexed from 1) H68 D92 G148 A150
Enzyme Commision number 2.7.7.48: RNA-directed RNA polymerase.
3.4.21.98: hepacivirin.
3.4.22.-
3.6.1.15: nucleoside-triphosphate phosphatase.
3.6.4.13: RNA helicase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SU3 A Q1041 F1043 H1057 V1078 D1081 R1123 I1132 L1135 K1136 G1137 A1139 F1154 K1155 A1156 A1157 Q52 F54 H68 V89 D92 R134 I143 L146 K147 G148 A150 F165 K166 A167 A168 MOAD: Ki=554nM
PDBbind-CN: -logKd/Ki=6.26,Ki=554nM
BS02 ZN A C1097 C1099 C1145 H1149 C108 C110 C156 H160
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

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Molecular Function
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Biological Process
External links
PDB RCSB:3su4, PDBe:3su4, PDBj:3su4
PDBsum3su4
PubMed22910833
UniProtP26664|POLG_HCV1 Genome polyprotein

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