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2K1Q

NMR structure of hepatitis c virus ns3 serine protease complexed with the non-covalently bound phenethylamide inhibitor

Summary for 2K1Q
Entry DOI10.2210/pdb2k1q/pdb
Related1bt7 1dwx
DescriptorNS3 PROTEASE, PHENETHYLAMIDE, ZINC ION (3 entities in total)
Functional Keywordsserine protease, ns3, hepatitis c virus, non covalent inhibitor, envelope protein, helicase, hydrolase, nucleotide-binding, rna replication, transmembrane, viral protein
Biological sourceHepatitis C virus
Total number of polymer chains2
Total formula weight20363.04
Authors
Eliseo, T.,Gallo, M.,Pennestri, M.,Bazzo, R.,Cicero, D.O. (deposition date: 2008-03-13, release date: 2009-02-03, Last modification date: 2023-11-15)
Primary citationGallo, M.,Pennestri, M.,Bottomley, M.J.,Barbato, G.,Eliseo, T.,Paci, M.,Narjes, F.,De Francesco, R.,Summa, V.,Koch, U.,Bazzo, R.,Cicero, D.O.
Binding of a noncovalent inhibitor exploiting the S' region stabilizes the hepatitis C virus NS3 protease conformation in the absence of cofactor.
J.Mol.Biol., 385:1142-1155, 2009
Cited by
PubMed: 19061898
DOI: 10.1016/j.jmb.2008.11.017
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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