› 2nnq

X-ray diffraction
1.8Å resolution

Crystal structure of human adipocyte fatty acid binding protein in complex with ((2'-(5-ethyl-3,4-diphenyl-1H-pyrazol-1-yl)-3-biphenylyl)oxy)acetic acid

Released:
DOI: 10.2210/pdb2nnq/pdb
PDB entry 2nnq coloured by chain, front view.
PDB entry 2nnq coloured by chain, side view.
PDB entry 2nnq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Potent and selective biphenyl azole inhibitors of adipocyte fatty acid binding protein (aFABP).
Sulsky R, Magnin DR, Huang Y, Simpkins L, Taunk P, Patel M, Zhu Y, Stouch TR, Bassolino-Klimas D, Parker R, Harrity T, Stoffel R, Taylor DS, Lavoie TB, Kish K, Jacobson BL, Sheriff S, Adam LP, Ewing WR, Robl JA
Bioorg Med Chem Lett 17 3511-5 (2007)
PMID: 17502136

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

2 bound ligands:
Ligand SO4 2 x SO4
Ligand T4B 1 x T4B
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 32.62Å b: 53.93Å c: 74.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.188 0.235
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Binding of small-molecule ligands to proteins: "what you see" is not always "what you get".
Mobley et al. (2009)
15 more

25 mentions without citation

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