1xct

X-ray diffraction
3.05Å resolution

Complex HCV core-Fab 19D9D6-Protein L mutant (D55A, L57H, Y64W) in space group P21212

Released:

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:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-210915 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Mature core protein Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 44 amino acids
Theoretical weight: 4.91 KDa
Source organism: Hepatitis C virus isolate HC-J8
Expression system: Not provided
UniProt:
  • Canonical: P26661 (Residues: 2-45; Coverage: 2%)
Sequence domains: Hepatitis C virus capsid protein
Monoclonal antibody 19D9D6 Light chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 220 amino acids
Theoretical weight: 24.33 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Monoclonal antibody 19D9D6 Heavy chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 218 amino acids
Theoretical weight: 23.56 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Protein L Chains: L, M
Molecule details ›
Chains: L, M
Length: 80 amino acids
Theoretical weight: 8.9 KDa
Source organism: Finegoldia magna ATCC 29328
Expression system: Escherichia coli
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 129.5Å b: 222.48Å c: 43.76Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.329
Expression systems:
  • Not provided
  • Escherichia coli