› 1hb6

X-ray diffraction
2Å resolution

Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form

Released:
DOI: 10.2210/pdb1hb6/pdb
PDB 1hb6 coloured by chain and viewed from the front.
PDB 1hb6 coloured by chain and viewed from the side.
PDB 1hb6 coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.
van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA
J Mol Biol 309 181-92 (2001)
PMID: 11491287

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA-binding protein Chain: A
Molecule details ›
Chain: A
Length: 86 amino acids
Theoretical weight: 9.93 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P07107 (Residues: 2-87; Coverage: 99%)
Gene name: DBI
Structure domains: Acyl-CoA Binding Protein

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 26.05Å b: 54.78Å c: 65.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.226
Expression system: Not provided

Quick links

Citations

5 review citations

Functional and Structural Diversity of Acyl-coA Binding Proteins in Oil Crops.
Raboanatahiry et al. (2018)
4 more

6 mentions without citation

Slow unfolded-state structuring in Acyl-CoA binding protein folding revealed by simulation and experiment.
Voelz et al. (2012)
5 more