› 4q0x

X-ray diffraction
2.9Å resolution

Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2

Released:
DOI: 10.2210/pdb4q0x/pdb
PDB entry 4q0x coloured by chain, front view.
PDB entry 4q0x coloured by chain, side view.
PDB entry 4q0x coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.
Deng L, Ma L, Virata ML, Zhong L, Yan H, Zhao Z, Struble E, Feinstone S, Alter H, Zhang P
Proc Natl Acad Sci U S A 111 10690-5 (2014)
PMID: 25002515

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:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-106876 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein Chain: H
Molecule details ›
Chain: H
Length: 219 amino acids
Theoretical weight: 23.69 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: Q99LC4 (Residues: 20-239; Coverage: 49%)
Gene name: Igh
Sequence domains:
Structure domains: Immunoglobulins
Ig-like domain-containing protein Chain: L
Molecule details ›
Chain: L
Length: 218 amino acids
Theoretical weight: 23.95 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: A2NHM3 (Residues: 1-218; Coverage: 100%)
Gene names: Igk-C, Igkc
Sequence domains:
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chain: E
Molecule details ›
Chain: E
Length: 26 amino acids
Theoretical weight: 2.94 KDa
UniProt:
  • Canonical: P27958 (Residues: 421-446; 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: P4322
Unit cell:
a: 49.991Å b: 49.991Å c: 390.585Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.221 0.285

Quick links

Citations

11 review citations

Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design.
Tarr et al. (2015)
10 more

9 mentions without citation

From Structural Studies to HCV Vaccine Design.
Yechezkel et al. (2021)
8 more