› 5d48

X-ray diffraction
1.81Å resolution

Crystal Structure of FABP4 in complex with 3-{5-cyclopropyl-3-(3,5-dimethyl-1H-pyrazol-4-yl)-2-[3-(propan-2-yloxy) phenyl]-1H-indol-1-yl}propanoic acid

Released:
DOI: 10.2210/pdb5d48/pdb
PDB entry 5d48 coloured by chain, front view.
PDB entry 5d48 coloured by chain, side view.
PDB entry 5d48 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interaction Analysis of FABP4 Inhibitors by X-ray Crystallography and Fragment Molecular Orbital Analysis.
Tagami U, Takahashi K, Igarashi S, Ejima C, Yoshida T, Takeshita S, Miyanaga W, Sugiki M, Tokumasu M, Hatanaka T, Kashiwagi T, Ishikawa K, Miyano H, Mizukoshi T
ACS Med Chem Lett 7 435-9 (2016)
PMID: 27096055

Function and Biology Details

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

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: 152 amino acids
Theoretical weight: 16.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15090 (Residues: 1-132; Coverage: 100%)
Gene name: FABP4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand L96 1 x L96
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 32.08Å b: 53.73Å c: 74.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.244
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Adipocyte fatty acid binding protein 4 (FABP4) inhibitors. A comprehensive systematic review.
Floresta et al. (2017)
5 other articles