Structure of PDB 6s0j Chain A

Receptor sequence
>6s0jA (length=433) Species: 64320 (Zika virus) [Search protein sequence]
HHHHHHMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTR
VVAAEMEEALRGLPVRYMTTTEIVDLMCHATFTSRLLQPIRVPNYNLYIM
DEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIM
DTEVEVPERAWSSGFDWVTDYSGKTVWFVPSVRNGNEIAACLTKAGKRVI
QLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVI
LDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDH
AHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVE
LMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRH
GEKRVLKPRWMDARVCSDHAALKSFKEFAAGKR
3D structure
PDB6s0j New MFx transition state analog reveals the molecular mechanism of ATP hydrolysis by the Zika virus NS3 helicase
ChainA
Resolution1.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.56: mRNA (guanine-N(7))-methyltransferase.
2.1.1.57: methyltransferase cap1.
2.7.7.48: RNA-directed RNA polymerase.
3.4.21.91: flavivirin.
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 KQB A P196 K200 E286 G415 R459 R462 P20 K24 E102 G231 R275 R278
BS02 ADP A G197 G199 K200 T201 R202 N417 R462 G21 G23 K24 T25 R26 N233 R278
Gene Ontology
Molecular Function
GO:0004386 helicase activity
GO:0005524 ATP binding

View graph for
Molecular Function
External links
PDB RCSB:6s0j, PDBe:6s0j, PDBj:6s0j
PDBsum6s0j
PubMed33717640
UniProtA0A024B7W1|POLG_ZIKVF Genome polyprotein

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