› 1ab0

X-ray diffraction
1.9Å resolution

C1G/V32D/F57H MUTANT OF MURINE ADIPOCYTE LIPID BINDING PROTEIN AT PH 4.5

Released:
DOI: 10.2210/pdb1ab0/pdb
PDB entry 1ab0 coloured by chain, front view.
PDB entry 1ab0 coloured by chain, side view.
PDB entry 1ab0 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Biochemical and crystallographic analyses of a portal mutant of the adipocyte lipid-binding protein.
Ory J, Kane CD, Simpson MA, Banaszak LJ, Bernlohr DA
J Biol Chem 272 9793-801 (1997)
PMID: 9092513

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137406 (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: 14.5 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04117 (Residues: 3-132; Coverage: 99%)
Gene names: Ap2, Fabp4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P43212
Unit cell:
a: 56.47Å b: 56.47Å c: 80.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.253
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Physiological properties and functions of intracellular fatty acid-binding proteins.
Coe et al. (1998)
2 more

3 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
2 more