Structure of PDB 1dy8 Chain A

Receptor sequence
>1dy8A (length=175) Species: 31645 (Hepatitis C virus (isolate Taiwan)) [Search protein sequence]
APITAYSQQTRGLLGCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNG
VCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSMTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHV
VGIFRAAVCTRGVAKAVDFIPVESM
3D structure
PDB1dy8 Inhibition of the Hepatitis C Virus Ns3/4A Protease the Crystal Structures of Two Protease-Inhibitor Complexes
ChainA
Resolution2.4 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) H57 D81 G137 S139
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 I3 T4 A5 Y6 S7 Q8 T10 T19 S20 Q28 D30 E32 V33 Q34 V35 L36 S37 K62 T63 L64 A65 I3 T4 A5 Y6 S7 Q8 T10 T19 S20 Q28 D30 E32 V33 Q34 V35 L36 S37 K62 T63 L64 A65
BS02 0F7 A H57 K136 G137 S139 F154 R155 A156 A157 D168 H57 K136 G137 S139 F154 R155 A156 A157 D168
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:1dy8, PDBe:1dy8, PDBj:1dy8
PDBsum1dy8
PubMed10702283
UniProtP26662|POLG_HCVJA Genome polyprotein

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