Structure of PDB 4a92 Chain A

Receptor sequence
>4a92A (length=639) [Search protein sequence]
GSVVIVGRIILSGSGSITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVV
STATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQ
APPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLK
GSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVESMETTMRSPVFTD
NSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATL
GFGAYMSKAHGIDPNIRTGVRTITTGAPVTYSTYGKFLADGGCSGGAYDI
IICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNI
EEVALSNTGEIPFYGKAIPIEAIRGGRHLIFCHSKKKCDELAAKLSGLGI
NAVAYYRGLDVSVIPTIGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTV
DFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYRFVTPGERPSGMF
DSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVF
TGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLI
RLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSA
3D structure
PDB4a92 A Macrocyclic Hcv Ns3/4A Protease Inhibitor Interacts with Protease and Helicase Residues in the Complex with its Full- Length Target.
ChainA
Resolution2.73 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T10 C16 H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) T24 C30 H71 D95 G151 S153
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 ZN A C97 C99 C145 C111 C113 C159
BS02 F9K A Q41 H57 G58 D81 R123 L135 K136 G137 S139 F154 R155 A156 A157 Q526 D527 H528 Q55 H71 G72 D95 R137 L149 K150 G151 S153 F168 R169 A170 A171 Q540 D541 H542
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4a92, PDBe:4a92, PDBj:4a92
PDBsum4a92
PubMed22160684
UniProtP26663|POLG_HCVBK Genome polyprotein

[Back to BioLiP]