2KWT
Solution structure of NS2 [27-59]
Summary for 2KWT
Entry DOI | 10.2210/pdb2kwt/pdb |
Related | 1JY0 |
NMR Information | BMRB: 16886 |
Descriptor | Protease NS2-3 (1 entity in total) |
Functional Keywords | hepatitis c virus, ns2 domain, membrane protein, viral protein |
Biological source | Hepatitis C virus (HCV) |
Cellular location | Core 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 (By similarity). RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): Q9WMX2 |
Total number of polymer chains | 1 |
Total formula weight | 4054.85 |
Authors | Montserret, R.,Bartenschlager, R.,Penin, F. (deposition date: 2010-04-19, release date: 2011-03-02, Last modification date: 2024-05-01) |
Primary citation | Jirasko, V.,Montserret, R.,Lee, J.Y.,Gouttenoire, J.,Moradpour, D.,Penin, F.,Bartenschlager, R. Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly. Plos Pathog., 6:e1001233-e1001233, 2010 Cited by PubMed: 21187906DOI: 10.1371/journal.ppat.1001233 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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