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3GPG

Crystal structure of macro domain of Chikungunya virus

Summary for 3GPG
Entry DOI10.2210/pdb3gpg/pdb
Related3GPO 3GPQ
DescriptorNon-structural protein 3 (2 entities in total)
Functional Keywordsmacro domain, x domain, chikungunya, alphavirus, virus, vizier. viral enzymes involved in replication, atp-binding, cell membrane, endosome, helicase, hydrolase, lipoprotein, lysosome, membrane, methyltransferase, mrna capping, mrna processing, multifunctional enzyme, nucleotide-binding, nucleotidyltransferase, nucleus, palmitate, phosphoprotein, protease, rna replication, rna-binding, rna-directed rna polymerase, thiol protease, transferase, viral protein
Biological sourceChikungunya virus
Cellular locationNon-structural polyprotein: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). P123: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). mRNA-capping enzyme nsP1: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Protease nsP2: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 3: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). RNA-directed RNA polymerase nsP4: Host endosome membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): Q8JUX6
Total number of polymer chains4
Total formula weight74540.49
Authors
Malet, H.,Jamal, S.,Coutard, B.,Canard, B. (deposition date: 2009-03-23, release date: 2009-07-21, Last modification date: 2024-02-21)
Primary citationMalet, H.,Coutard, B.,Jamal, S.,Dutartre, H.,Papageorgiou, N.,Neuvonen, M.,Ahola, T.,Forrester, N.,Gould, E.A.,Lafitte, D.,Ferron, F.,Lescar, J.,Gorbalenya, A.E.,de Lamballerie, X.,Canard, B.
The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket
J.Virol., 83:6534-6545, 2009
Cited by
PubMed: 19386706
DOI: 10.1128/JVI.00189-09
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

218500

數據於2024-04-17公開中

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