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THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES
Summary
Header HYDROLASEsearch
Method SOLUTION NMR
Experiment Spacegroup: P 1
Released 22/06/1999, deposition: 01/09/1998, last revision: 24/02/2009
Authors Barbato, G.search; Cicero, D.O.search; Nardi, M.C.search; Steinkuhler, C.search; Cortese, R.search; De Francesco, R.search; Bazzo, R.search
Primary citation The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism.
J.MOL.BIOL.search vol:289, pag:371-384 (1999) [PubMed ID 10366511 ]search
Keywords HYDROLASEsearch, VIRAL NON-STRUCTURAL PROTEINsearch, SERINE PROTEASEsearch
EC 2.7.7.48 ExPASy BRENDA search 3.4.21.98 ExPASy BRENDA search 3.6.1.15 ExPASy BRENDA search (A)
Organism Hepatitis C virus 11103search(A)
UniProt Genome polyprotein [Contains: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (EC 3.4.22.-) (p23); Serine protease/NTPase/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.1.-) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)] P26663search (A)
Polymers
Id Name Type UniProt Residues Observed
A NS3 SERINE PROTEASE Protein P26663 (POLG_HCVBK)search
 186 88%
Heterogens
Id Name Ligands
A ZINC ION ZN search
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