› 3mlt

X-ray diffraction
2.49Å resolution

Crystal structure of anti-HIV-1 V3 Fab 2557 in complex with a UG1033 V3 peptide

Released:
DOI: 10.2210/pdb3mlt/pdb
PDB entry 3mlt coloured by chain, front view.
PDB entry 3mlt coloured by chain, side view.
PDB entry 3mlt coloured by chain, top view.
Source organisms:
Primary publication:
Conserved structural elements in the V3 crown of HIV-1 gp120.
Jiang X, Burke V, Totrov M, Williams C, Cardozo T, Gorny MK, Zolla-Pazner S, Kong XP
Nat Struct Mol Biol 17 955-61 (2010)
PMID: 20622876

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-212860 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Human monoclonal anti-HIV-1 gp120 V3 antibody 2557 Fab light chain Chains: A, D, G, L
Molecule details ›
Chains: A, D, G, L
Length: 219 amino acids
Theoretical weight: 23.33 KDa
Source organism: Homo sapiens
Structure domains: Immunoglobulins
Human monoclonal anti-HIV-1 gp120 V3 antibody 2557 Fab heavy chain Chains: B, E, H, I
Molecule details ›
Chains: B, E, H, I
Length: 226 amino acids
Theoretical weight: 24.19 KDa
Source organism: Homo sapiens
Structure domains: Immunoglobulins
Human immunodeficiency virus 1 envelope glycoprotein Gp120 domain-containing protein Chains: C, P
Molecule details ›
Chains: C, P
Length: 23 amino acids
Theoretical weight: 2.46 KDa
Source organism: Human immunodeficiency virus 1
UniProt:
  • Canonical: Q9WNX3 (Residues: 38-60; Coverage: 20%)
Gene name: env

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21
Unit cell:
a: 75.683Å b: 142.927Å c: 85.013Å
α: 90° β: 95° γ: 90°
R-values:
R R work R free
0.206 0.202 0.28

Quick links

Citations

2 review citations

Requirements for empirical immunogenicity trials, rather than structure-based design, for developing an effective HIV vaccine.
Van Regenmortel MH. (2012)
1 more

5 mentions without citation

Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction.
Zhu et al. (2014)
4 more