› 5te7

X-ray diffraction
2.15Å 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-231368 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Heavy chain of N6 Chain: H
Molecule details ›
Chain: H
Length: 225 amino acids
Theoretical weight: 24.19 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Light chain of N6 Chain: L
Molecule details ›
Chain: L
Length: 210 amino acids
Theoretical weight: 23.16 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Envelope glycoprotein gp160 Chain: G
Molecule details ›
Chain: G
Length: 350 amino acids
Theoretical weight: 38.99 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Homo sapiens
UniProt:
  • Canonical: Q202J8 (Residues: 43-489; Coverage: 41%)
Gene name: env
Sequence domains: Envelope glycoprotein GP120
Structure domains: Human immunodeficiency virus 1, Gp160, envelope glycoprotein

Ligands and Environments

3 bound ligands:
Ligand EPE 2 x EPE
Ligand EDO 7 x EDO
Ligand NAG 8 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 62.675Å b: 65.547Å c: 241.522Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.228
Expression system: Homo sapiens

Quick links

Citations

54 review citations

Recent progress in broadly neutralizing antibodies to HIV.
Sok et al. (2018)
53 more

7 mentions without citation

Identification of a CD4-Binding-Site Antibody to HIV that Evolved Near-Pan Neutralization Breadth.
Huang et al. (2016)
6 more