Function and Biology Details
Reaction catalysed:
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- 6-phosphogluconate dehydrogenase, domain 2
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal
- 6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily
- 3-hydroxyacyl-CoA dehydrogenase, conserved site
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding
- NAD(P)-binding domain superfamily
- 3-hydroxyacyl-CoA dehydrogenase
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
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 33.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
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%)
Sequence domains:
- 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain
- 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 19-ID
Spacegroup:
P212121
Expression system: Escherichia coli
