› 2hnx

X-ray diffraction
1.5Å resolution

Crystal Structure of aP2

Released:
DOI: 10.2210/pdb2hnx/pdb
PDB entry 2hnx coloured by chain, front view.
PDB entry 2hnx coloured by chain, side view.
PDB entry 2hnx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2).
Marr E, Tardie M, Carty M, Brown Phillips T, Wang IK, Soeller W, Qiu X, Karam G
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 1058-60 (2006)
PMID: 17077479

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: 136 amino acids
Theoretical weight: 15.18 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

3 bound ligands:
Ligand PO4 1 x PO4
Ligand PLM 1 x PLM
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 32.47Å b: 53.94Å c: 75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Role of the fatty acid-binding protein 4 in heart failure and cardiovascular disease.
Rodríguez-Calvo et al. (2017)
1 more

8 mentions without citation

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