› 1bwy

Solution NMR

NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN

Released:
DOI: 10.2210/pdb1bwy/pdb
PDB entry 1bwy coloured by chain, ensemble of 25 models, front view.
PDB entry 1bwy coloured by chain, ensemble of 25 models, side view.
PDB entry 1bwy coloured by chain, ensemble of 25 models, top view.
Source organism: Bos taurus
Primary publication:
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
Lassen D, Lücke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Rüterjans H
Eur J Biochem 230 266-80 (1995)
PMID: 7601110

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-145453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid-binding protein, heart Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.67 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10790 (Residues: 2-133; Coverage: 99%)
Gene name: FABP3
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: DISTANCE GEOMETRY, ENERGY MINIMIZATION
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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