7jtf

X-ray diffraction
3.35Å resolution

Structure of Hepatitis C Virus Envelope Glycoprotein E2 core from genotype 6a bound to broadly neutralizing antibody RM2-01

Released:

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-207694 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
RM2-01 Fab heavy chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 229 amino acids
Theoretical weight: 24.11 KDa
Source organism: Macaca mulatta
Expression system: Homo sapiens
RM2-01 Fab light chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 214 amino acids
Theoretical weight: 23.45 KDa
Source organism: Macaca mulatta
Expression system: Homo sapiens
Envelope glycoprotein E2 Chains: E, F
Molecule details ›
Chains: E, F
Length: 189 amino acids
Theoretical weight: 20.71 KDa
Source organism: Recombinant Hepatitis C virus HK6a/JFH-1
Expression system: Homo sapiens
UniProt:
  • Canonical: B9V0E2 (Residues: 412-459, 488-570, 588-590, 604-651; Coverage: 6%)
Sequence domains: Hepatitis C virus non-structural protein E2/NS1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 89.732Å b: 64.887Å c: 145.208Å
α: 90° β: 105.155° γ: 90°
R-values:
R R work R free
0.245 0.242 0.296
Expression system: Homo sapiens