› 1lif

X-ray diffraction
1.6Å resolution

THE ADIPOCYTE LIPID-BINDING PROTEIN AT 1.6 ANGSTROMS RESOLUTION: CRYSTAL STRUCTURES OF THE APOPROTEIN AND WITH BOUND SATURATED AND UNSATURATED FATTY ACIDS

Released:
DOI: 10.2210/pdb1lif/pdb
PDB entry 1lif coloured by chain, front view.
PDB entry 1lif coloured by chain, side view.
PDB entry 1lif coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The adipocyte lipid-binding protein at 1.6-A resolution. Crystal structures of the apoprotein and with bound saturated and unsaturated fatty acids.
Xu Z, Bernlohr DA, Banaszak LJ
J Biol Chem 268 7874-84 (1993)
PMID: 8463311

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid-binding protein, adipocyte Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 14.54 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04117 (Residues: 2-132; Coverage: 99%)
Gene names: Ap2, Fabp4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand STE 1 x STE
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 120.53Å b: 37.86Å c: 28.73Å
α: 90° β: 92.49° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Escherichia coli

Quick links

Citations

17 review citations

The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism.
Chmurzyńska A. (2006)
16 more

7 mentions without citation

Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock.
Bikadi et al. (2009)
6 more