› 1m75

X-ray diffraction
2.3Å resolution

Crystal Structure of the N208S Mutant of L-3-Hydroxyacyl-COA Dehydrogenase in Complex with NAD and Acetoacetyl-COA

Released:
DOI: 10.2210/pdb1m75/pdb
PDB entry 1m75 coloured by chain, front view.
PDB entry 1m75 coloured by chain, side view.
PDB entry 1m75 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Barycki JJ, Banaszak LJ

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: 302 amino acids
Theoretical weight: 32.84 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


Cofactor: Ligand NAD 2 x NAD
1 bound ligand:
Ligand CAA 2 x CAA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 50.151Å b: 87.597Å c: 158.545Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.279
Expression system: Escherichia coli

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