› 3fr5

X-ray diffraction
2.2Å resolution

N-Benzyl-indolo carboxylic acids: Design and synthesis of potent and selective adipocyte Fatty-Acid Binding Protein (A-FABP) inhibitors

Released:
DOI: 10.2210/pdb3fr5/pdb
PDB entry 3fr5 coloured by chain, front view.
PDB entry 3fr5 coloured by chain, side view.
PDB entry 3fr5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
N-Benzyl-indolo carboxylic acids: Design and synthesis of potent and selective adipocyte fatty-acid binding protein (A-FABP) inhibitors.
Barf T, Lehmann F, Hammer K, Haile S, Axen E, Medina C, Uppenberg J, Svensson S, Rondahl L, Lundbäck T
Bioorg Med Chem Lett 19 1745-8 (2009)
PMID: 19217286

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: 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 I4A 1 x I4A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21212
Unit cell:
a: 71.715Å b: 53.384Å c: 32.097Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.274
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Metabolic functions of FABPs--mechanisms and therapeutic implications.
Hotamisligil et al. (2015)
7 more

3 mentions without citation

Binding modes of three inhibitors 8CA, F8A and I4A to A-FABP studied based on molecular dynamics simulation.
Chen et al. (2014)
2 more