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1A1V

HEPATITIS C VIRUS NS3 HELICASE DOMAIN COMPLEXED WITH SINGLE STRANDED SDNA

Summary for 1A1V
Entry DOI10.2210/pdb1a1v/pdb
DescriptorDNA (5'-D(*UP*UP*UP*UP*UP*UP*UP*U)-3'), PROTEIN (NS3 PROTEIN), SULFATE ION, ... (4 entities in total)
Functional Keywordshepatitis c virus, rna helicase, nonstructural proteins, single-stranded dna, hydrolase-dna complex, hydrolase/dna
Biological sourceHepatitis C virus (isolate H)
More
Cellular locationCore 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 : P27958
Total number of polymer chains2
Total formula weight53734.73
Authors
Kim, J.L.,Morgenstern, K.A.,Griffith, J.P.,Dwyer, M.D.,Thomson, J.A.,Murcko, M.A.,Lin, C.,Caron, P.R. (deposition date: 1997-12-17, release date: 1999-01-13, Last modification date: 2011-07-13)
Primary citationKim, J.L.,Morgenstern, K.A.,Griffith, J.P.,Dwyer, M.D.,Thomson, J.A.,Murcko, M.A.,Lin, C.,Caron, P.R.
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.
Structure, 6:89-100, 1998
Cited by
PubMed: 9493270
DOI: 10.1016/S0969-2126(98)00010-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

218500

數據於2024-04-17公開中

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