› 1f12

X-ray diffraction
2.4Å resolution

L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH 3-HYDROXYBUTYRYL-COA

Released:
DOI: 10.2210/pdb1f12/pdb
PDB entry 1f12 coloured by chain, front view.
PDB entry 1f12 coloured by chain, side view.
PDB entry 1f12 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase.
Barycki JJ, O'Brien LK, Strauss AW, Banaszak LJ
J Biol Chem 275 27186-96 (2000)
PMID: 10840044

Function and Biology Details

Reaction catalysed: 
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 33.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16836 (Residues: 13-314; Coverage: 96%)
Gene names: HAD, HAD1, HADH, HADHSC, SCHAD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 3HC 1 x 3HC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 50.04Å b: 88.1Å c: 167.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.265
Expression system: Escherichia coli

Quick links

Citations

2 review citations

3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease.
Yang et al. (2005)
1 more

6 mentions without citation

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.
Ishikawa et al. (2004)
5 more