5kzp

X-ray diffraction
2.26Å resolution

Structure of the HCV1-C1 Antibody-Antigen Complex

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-210920 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HCV1-C1 Antibody Fab Heavy Chain Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 226 amino acids
Theoretical weight: 24.58 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
HCV1-C1 Antibody Fab Light Chain Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 213 amino acids
Theoretical weight: 23.4 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 15 amino acids
Theoretical weight: 1.73 KDa
UniProt:
  • Canonical: P26663 (Residues: 412-423; Coverage: 0%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 47.07Å b: 94.538Å c: 126.758Å
α: 91.84° β: 94.95° γ: 97.91°
R-values:
R R work R free
0.22 0.218 0.261
Expression system: Homo sapiens