1cwx

Solution NMR

SOLUTION STRUCTURE OF THE HEPATITIS C VIRUS N-TERMINAL CAPSID PROTEIN 2-45 [C-HCV(2-45)]

Released:
Entry authors: Ladaviere L, Deleage G, Montserret R, Dalbon P, Jolivet M, Penin F

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151107 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mature core protein Chain: A
Molecule details ›
Chain: A
Length: 44 amino acids
Theoretical weight: 4.91 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided
UniProt:
  • Canonical: P27958 (Residues: 2-45; Coverage: 2%)
Sequence domains: Hepatitis C virus capsid protein
Structure domains: Hepatitis C Virus Capsid Protein; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY SIMULATED ANNEALING MOLECULAR DYNAMICS MATRIX RELAXATION
Expression system: Not provided