› 1ifc

X-ray diffraction
1.19Å resolution

REFINEMENT OF THE STRUCTURE OF RECOMBINANT RAT INTESTINAL FATTY ACID-BINDING APOPROTEIN AT 1.2 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1ifc/pdb
PDB entry 1ifc coloured by chain, front view.
PDB entry 1ifc coloured by chain, side view.
PDB entry 1ifc coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-A resolution.
Scapin G, Gordon JI, Sacchettini JC
J Biol Chem 267 4253-69 (1992)
PMID: 1740465

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: 132 amino acids
Theoretical weight: 15.15 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: P02693 (Residues: 1-132; Coverage: 100%)
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: 35.83Å b: 51.42Å c: 31.34Å
α: 90° β: 91.44° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Not provided

Quick links

Citations

12 review citations

Cellular fatty acid-binding proteins: their function and physiological significance.
Glatz et al. (1996)
11 more

36 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
35 more