› 1ifb

X-ray diffraction
1.96Å resolution

REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1ifb/pdb
PDB entry 1ifb coloured by chain, front view.
PDB entry 1ifb coloured by chain, side view.
PDB entry 1ifb coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli.
Sacchettini JC, Gordon JI, Banaszak LJ
Proc Natl Acad Sci U S A 86 7736-40 (1989)
PMID: 2682622

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-136051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid-binding protein, intestinal Chain: A
Molecule details ›
Chain: A
Length: 131 amino acids
Theoretical weight: 15.02 KDa
Source organism: Rattus rattus
Expression system: Not provided
UniProt:
  • Canonical: P02693 (Residues: 2-132; Coverage: 99%)
Gene names: Fabp2, Fabpi
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
Spacegroup: P21
Unit cell:
a: 36Å b: 56.6Å c: 31.6Å
α: 90° β: 113.1° γ: 90°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Not provided

Quick links

Citations

8 review citations

The emerging functions and mechanisms of mammalian fatty acid-binding proteins.
Storch et al. (2008)
7 more

18 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
17 more