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2RNK

NMR structure of the domain 513-651 of the SARS-CoV nonstructural protein nsp3

Replaces:  2JWI
Summary for 2RNK
Entry DOI10.2210/pdb2rnk/pdb
Related2JZD 2JZE 2JZF
DescriptorReplicase polyprotein 1ab (1 entity in total)
Functional Keywordssars-cov, sars-unique domain, nonstructural protein, nsp3, nsp3c, functional and structural proteomics of sars-cov-related proteins, fsps, psi-2, protein structure initiative, joint center for structural genomics, jcsg, atp-binding, cytoplasm, endonuclease, exonuclease, helicase, hydrolase, membrane, metal-binding, nuclease, nucleotide-binding, nucleotidyltransferase, protease, ribosomal frameshift, rna replication, rna-binding, rna-directed rna polymerase, thiol protease, transferase, transmembrane, zinc, zinc-finger, viral protein
Biological sourceSARS coronavirus
Cellular locationNon-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641
Total number of polymer chains1
Total formula weight15859.38
Authors
Primary citationChatterjee, A.,Johnson, M.A.,Serrano, P.,Pedrini, B.,Joseph, J.S.,Neuman, B.W.,Saikatendu, K.,Buchmeier, M.J.,Kuhn, P.,Wuthrich, K.
Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold.
J.Virol., 83:1823-1836, 2009
Cited by
PubMed: 19052085
DOI: 10.1128/JVI.01781-08
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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