› 4dgv

X-ray diffraction
1.8Å resolution

Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody HCV1, P2(1) form

Released:
DOI: 10.2210/pdb4dgv/pdb
PDB entry 4dgv coloured by chain, front view.
PDB entry 4dgv coloured by chain, side view.
PDB entry 4dgv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1.
Kong L, Giang E, Robbins JB, Stanfield RL, Burton DR, Wilson IA, Law M
Proc Natl Acad Sci U S A 109 9499-504 (2012)
PMID: 22623528

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-210918 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HCV1 Heavy Chain Chain: H
Molecule details ›
Chain: H
Length: 226 amino acids
Theoretical weight: 24.58 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
HCV1 Light Chain Chain: L
Molecule details ›
Chain: L
Length: 213 amino acids
Theoretical weight: 23.4 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.55 KDa
UniProt:
  • Canonical: P26663 (Residues: 412-423; Coverage: 0%)

Ligands and Environments

2 bound ligands:
Ligand NA 1 x NA
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 44.041Å b: 75.301Å c: 60.8Å
α: 90° β: 91.53° γ: 90°
R-values:
R R work R free
0.172 0.17 0.214
Expression system: Homo sapiens

Quick links

Citations

33 review citations

Current progress in development of hepatitis C virus vaccines.
Liang TJ. (2013)
32 more

15 mentions without citation

Conformational Flexibility in the CD81-Binding Site of the Hepatitis C Virus Glycoprotein E2.
Ströh et al. (2018)
14 more