› 4om0

X-ray diffraction
2.29Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-211983 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Envelope glycoprotein gp160 Chain: G
Molecule details ›
Chain: G
Length: 353 amino acids
Theoretical weight: 39.21 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Homo sapiens
UniProt:
  • Canonical: Q0ED31 (Residues: 43-122, 201-303, 325-486; Coverage: 40%)
Gene name: env
Sequence domains: Envelope glycoprotein GP120
Structure domains: Human immunodeficiency virus 1, Gp160, envelope glycoprotein
Antigen binding fragment of heavy chain: Antibody VRC01 Chain: H
Molecule details ›
Chain: H
Length: 228 amino acids
Theoretical weight: 25.03 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Antigen binding fragment of light chain: Antibody VRC01 Chain: L
Molecule details ›
Chain: L
Length: 210 amino acids
Theoretical weight: 23.1 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand NAG 10 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 68.9Å b: 75.528Å c: 198.292Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.247
Expression system: Homo sapiens

Quick links

Citations

51 review citations

Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.
Burton et al. (2016)
50 more

1 mention without citation

Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro improves protection against lentiviral infection in vivo.
Rudicell et al. (2014)