› 2qv1

X-ray diffraction
2.4Å resolution

Crystal structure of HCV NS3-4A V36M mutant

Released:
DOI: 10.2210/pdb2qv1/pdb
PDB entry 2qv1 coloured by chain, front view.
PDB entry 2qv1 coloured by chain, side view.
PDB entry 2qv1 coloured by chain, top view.
Source organisms:
Entry author: Wei Y

Function and Biology Details

Reactions catalysed: 
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
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'.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106764 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 19.21 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
  • Canonical: A1Z093 (Residues: 1-181; Coverage: 29%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: C, D
Molecule details ›
Chains: C, D
Length: 21 amino acids
Theoretical weight: 2.08 KDa
Source organism: Hepatitis C virus (isolate H77)
Expression system: Not provided
UniProt:
  • Canonical: P27958 (Residues: 1678-1696; Coverage: 1%)
Sequence domains: Hepatitis C virus non-structural protein NS4a

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: R32
Unit cell:
a: 228.76Å b: 228.76Å c: 75.53Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.265
Expression systems:
  • Escherichia coli
  • Not provided

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