Structure of PDB 4b75 Chain B

Receptor sequence
>4b75B (length=642) Species: 11105 (Hepatitis C virus (isolate BK)) [Search protein sequence]
GSVVIVGRIILSSITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVVSTA
TQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPP
GARSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSS
GGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVESMETTMRSPVFTDNSS
PPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFG
AYMSKAHGIDPNIRTGVRTITTGAPVTYSTYGKFLADGGCSGGAYDIIIC
DECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEV
ALSNTGEIPFYGKAIPIEAIRGGRHLIFCHSKKKCDELAAKLSGLGINAV
AYYRGLDVSVIPTIGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFS
LDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYRFVTPGERPSGMFDSS
VLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGL
THIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLK
PTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVLT
3D structure
PDB4b75 Discovery of an Allosteric Mechanism for the Regulation of Hcv Ns3 Protein Function.
ChainB
Resolution2.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T10 C16 H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) T21 C27 H68 D92 G148 S150
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 4VA B V78 D79 D81 R155 M485 F486 L517 V524 C525 Q526 L630 V89 D90 D92 R166 M496 F497 L528 V535 C536 Q537 L641
Gene Ontology
Molecular Function
GO:0004386 helicase activity
GO:0005524 ATP binding
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:4b75, PDBe:4b75, PDBj:4b75
PDBsum4b75
PubMed23023261
UniProtP26663|POLG_HCVBK Genome polyprotein

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