› 4hzl

X-ray diffraction
2.85Å resolution

Neutralizing antibody mAb#8 in complex with the Epitope II of HCV E2 envelope protein

Released:
DOI: 10.2210/pdb4hzl/pdb
PDB entry 4hzl coloured by chain, front view.
PDB entry 4hzl coloured by chain, side view.
PDB entry 4hzl coloured by chain, top view.
Source organisms:
Primary publication:
Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus.
Deng L, Zhong L, Struble E, Duan H, Ma L, Harman C, Yan H, Virata ML, Zhao Z, Feinstone S, Alter H, Zhang P
Proc Natl Acad Sci U S A 110 7418-22 (2013)
PMID: 23589879

Function and Biology Details

Reactions catalysed: 
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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-207847 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Fab heavy chain Chains: A, H
Molecule details ›
Chains: A, H
Length: 222 amino acids
Theoretical weight: 23.74 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Fab light chain Chains: B, L
Molecule details ›
Chains: B, L
Length: 217 amino acids
Theoretical weight: 23.88 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
E2 envelop protein Chains: E, F
Molecule details ›
Chains: E, F
Length: 17 amino acids
Theoretical weight: 1.98 KDa
Source organism: Recombinant Hepatitis C virus H77(5'UTR-NS2)/JFH1_V787A,Q1247L
UniProt:
  • Canonical: F5BWY6 (Residues: 430-446; Coverage: 1%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P43212
Unit cell:
a: 137.252Å b: 137.252Å c: 140.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.277

Quick links

Citations

13 review citations

The past, present and future of neutralizing antibodies for hepatitis C virus.
Ball et al. (2014)
12 more

12 mentions without citation

Viral evasion and challenges of hepatitis C virus vaccine development.
Pierce et al. (2016)
11 more