› 1hms

X-ray diffraction
1.4Å resolution

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

Released:
DOI: 10.2210/pdb1hms/pdb
PDB entry 1hms coloured by chain, front view.
PDB entry 1hms coloured by chain, side view.
PDB entry 1hms coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids.
Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC
Structure 2 523-34 (1994)
PMID: 7922029

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-138660 (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: 14.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05413 (Residues: 2-133; Coverage: 99%)
Gene names: FABP11, FABP3, MDGI
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand OLA 1 x OLA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 34.65Å b: 55.45Å c: 71.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.121 0.121 not available
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

9 mentions without citation

Tissue-specific functions in the fatty acid-binding protein family.
Storch et al. (2010)
8 more