PDBe 3had

X-ray diffraction
2Å resolution

BIOCHEMICAL CHARACTERIZATION AND STRUCTURE DETERMINATION OF HUMAN HEART SHORT CHAIN L-3-HYDROXYACYL COA DEHYDROGENASE PROVIDE INSIGHT INTO CATALYTIC MECHANISM

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 33.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16836 (Residues: 13-314; Coverage: 96%)
Gene names: HAD, HADH, HADHSC, SCHAD
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 50.23Å b: 86.02Å c: 167.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.264
Expression system: Escherichia coli