› 1ael

Solution NMR

NMR STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1ael/pdb
PDB entry 1ael coloured by chain, ensemble of 20 models, front view.
PDB entry 1ael coloured by chain, ensemble of 20 models, side view.
PDB entry 1ael coloured by chain, ensemble of 20 models, top view.
Source organism: Rattus norvegicus
Primary publication:
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Hodsdon ME, Cistola DP
Biochemistry 36 2278-90 (1997)
PMID: 9047330

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 norvegicus
Expression system: Escherichia coli str. K-12 substr. MG1655
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
Refinement method: SIMULATED ANNEALING REFINEMENT
Expression system: Escherichia coli str. K-12 substr. MG1655

Quick links

Citations

16 review citations

The fatty acid transport function of fatty acid-binding proteins.
Storch et al. (2000)
15 more

9 mentions without citation

Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins.
Toke O. (2022)
8 more