› 1tou

X-ray diffraction
2Å resolution

Crystal structure of human adipocyte fatty acid binding protein in complex with a non-covalent ligand

Released:
DOI: 10.2210/pdb1tou/pdb
PDB entry 1tou coloured by chain, front view.
PDB entry 1tou coloured by chain, side view.
PDB entry 1tou coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substituted benzylamino-6-(trifluoromethyl)pyrimidin-4(1H)-ones: a novel class of selective human A-FABP inhibitors.
Ringom R, Axen E, Uppenberg J, Lundbäck T, Rondahl L, Barf T
Bioorg Med Chem Lett 14 4449-52 (2004)
PMID: 15357970

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147213 (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: 14.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15090 (Residues: 2-132; Coverage: 99%)
Gene name: FABP4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand B1V 1 x B1V
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 71.829Å b: 53.106Å c: 31.383Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.2 0.279
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Fatty Acid-Binding Protein 4 (FABP4): Pathophysiological Insights and Potent Clinical Biomarker of Metabolic and Cardiovascular Diseases.
Furuhashi et al. (2014)
5 more

5 mentions without citation

Fatty acid-binding proteins: role in metabolic diseases and potential as drug targets.
Furuhashi et al. (2008)
4 more