Structure of PDB 4n0o Chain E Binding Site BS02
Receptor Information
>4n0o Chain E (length=396) Species:
299386
(Equine arteritis virus Bucyrus) [
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AVCTVCGAAPVAKSACGGWFCGNCVPYHAGHCHTTSLFACGHDIMYRSTY
CTMCEGSPKQMVPKVPHPILDHLLCHIDYGSKEELTLVVADGTTSPPGRY
KVGHKVVAVVADVGGNIVFGCPGSHIVPLQDTLKGVVVNKALKNAAASEY
VEGPPGSGKTFHLVKDVLAVVGSATLVVPTHASMLDCINKLKQAGADPYF
VVPKYTVLDFPRPGSGNITVRLPQVGTSEGETFVDEVAYFSPVDLARILT
QGRVKGYGDLNQLGCVGPASVPRNLWLRHFVSLEPLRVCHRFGAAVCDLI
KGIYPYYEPAPHTTKVVFVPNPDFEKGVVITAYHKDRGLGHRTIDSIQGC
TFPVVTLRLPTPQSLTRPRAVVAVTRASQELYIYDPFDQLSGLLKF
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
4n0o Chain E Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
4n0o
Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase.
Resolution
2.65 Å
Binding residue
(original residue number in PDB)
H29 H32 C33
Binding residue
(residue number reindexed from 1)
H28 H31 C32
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.7.7.48
: RNA-directed RNA polymerase.
3.4.19.12
: ubiquitinyl hydrolase 1.
3.4.21.-
3.4.22.-
3.6.4.12
: DNA helicase.
3.6.4.13
: RNA helicase.
4.6.1.-
Gene Ontology
Molecular Function
GO:0005524
ATP binding
GO:0008270
zinc ion binding
View graph for
Molecular Function
External links
PDB
RCSB:4n0o
,
PDBe:4n0o
,
PDBj:4n0o
PDBsum
4n0o
PubMed
24369429
UniProt
P19811
|RPOA_EAVBU Replicase polyprotein 1ab (Gene Name=rep)
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