1GX5
Hepatitis C Virus RNA Polymerase in Complex with GTP and Manganese
Summary for 1GX5
Entry DOI | 10.2210/pdb1gx5/pdb |
Related | 1C2P 1CSJ 1CU1 1NS3 1QUV 8OHM |
Descriptor | RNA-DIRECTED RNA POLYMERASE, GUANOSINE-5'-TRIPHOSPHATE, MANGANESE (II) ION, ... (4 entities in total) |
Functional Keywords | transferase, polyprotein, glycoprotein, rna-directed rna polymerase, core protein, coat protein, envelope protein, helicase, atp binding, transmembrane, nonstructural protein |
Biological source | HEPATITIS C VIRUS (ISOLATE BK) (HCV) |
Cellular location | Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein. Core protein p19: Virion . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . p7: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protease NS2-3: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Serine protease NS3: Host endoplasmic reticulum membrane ; Peripheral membrane protein . Non-structural protein 4A: Host endoplasmic reticulum membrane ; Single-pass type I membrane protein . Non-structural protein 4B: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . 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 : P26663 |
Total number of polymer chains | 1 |
Total formula weight | 61415.43 |
Authors | Bressanelli, S.,Rey, F.A. (deposition date: 2002-03-27, release date: 2002-04-09, Last modification date: 2023-12-13) |
Primary citation | Bressanelli, S.,Tomei, L.,Rey, F.A.,De Francesco, R. A Structural Analysis of the Hepatitis C Virus RNA Polymerase in Complex with Ribonucleotides J.Virol., 76:3482-, 2002 Cited by PubMed: 11884572DOI: 10.1128/JVI.76.7.3482-3492.2002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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