Structure of PDB 1w3c Chain A

Receptor sequence
>1w3cA (length=173) Species: 11104 (Hepatitis C virus (isolate 1)) [Search protein sequence]
ITAYSQQTRGLLGCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNGVC
WTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSMTPCTCGSS
DLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHVVG
IFRAAVCTRGVAKAVDFIPVESM
3D structure
PDB1w3c The Design and Enzyme-Bound Crystal Structure of Indoline Based Peptidomimetic Inhibitors of Hepatitis C Virus Ns3 Protease
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) H55 D79 G135 S137
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 peptide A T4 A5 Y6 S7 Q8 T10 R11 C16 T19 S20 D30 G31 E32 V33 Q34 V35 L36 S37 K62 T63 M94 T2 A3 Y4 S5 Q6 T8 R9 C14 T17 S18 D28 G29 E30 V31 Q32 V33 L34 S35 K60 T61 M92
BS02 DN1 A H57 K136 G137 S138 S139 R155 A156 A157 C159 H55 K134 G135 S136 S137 R153 A154 A155 C157
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:1w3c, PDBe:1w3c, PDBj:1w3c
PDBsum1w3c
PubMed15588076
UniProtP26662|POLG_HCVJA Genome polyprotein

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