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4I33

Crystal structure of HCV NS3/4A R155K protease complexed with compound 4

Summary for 4I33
Entry DOI10.2210/pdb4i33/pdb
DescriptorGenome polyprotein, HCV non-structural protein 4A, SODIUM ION, ... (5 entities in total)
Functional Keywordshepatitis c virus, ns3, ns4a, protein-inhibitor complex compound 4, serine protease, r155k, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHepatitis C virus (HCV)
More
Cellular locationCore protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P26662 P26662
Total number of polymer chains4
Total formula weight44846.07
Authors
Lemke, C.T. (deposition date: 2012-11-23, release date: 2013-01-02, Last modification date: 2013-03-13)
Primary citationO'Meara, J.A.,Lemke, C.T.,Godbout, C.,Kukolj, G.,Lagace, L.,Moreau, B.,Thibeault, D.,White, P.W.,Llinas-Brunet, M.
Molecular Mechanism by Which a Potent Hepatitis C Virus NS3-NS4A Protease Inhibitor Overcomes Emergence of Resistance.
J.Biol.Chem., 288:5673-5681, 2013
Cited by
PubMed: 23271737
DOI: 10.1074/jbc.M112.439455
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9001 Å)
Structure validation

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