› 5y12

X-ray diffraction
1.75Å resolution

Crystal structure of human FABP4 complexed with ligand 5-((4-methoxynaphthalene)-1-sulfonamido)pentanoic acid

Released:
DOI: 10.2210/pdb5y12/pdb
PDB entry 5y12 coloured by chain, front view.
PDB entry 5y12 coloured by chain, side view.
PDB entry 5y12 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
From hit to lead: Structure-based discovery of naphthalene-1-sulfonamide derivatives as potent and selective inhibitors of fatty acid binding protein 4.
Gao DD, Dou HX, Su HX, Zhang MM, Wang T, Liu QF, Cai HY, Ding HP, Yang Z, Zhu WL, Xu YC, Wang HY, Li YX
Eur J Med Chem 154 44-59 (2018)
PMID: 29775936

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 BL21(DE3)
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

1 bound ligand:
Ligand 8JX 1 x 8JX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P212121
Unit cell:
a: 32.56Å b: 53.61Å c: 75.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.17 0.2
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Exogenous FABP4 interferes with differentiation, promotes lipolysis and inflammation in adipocytes.
Dou et al. (2020)
4 more

1 mention without citation

Steered Molecular Dynamics Simulations Study on FABP4 Inhibitors.
Tomarchio et al. (2023)