PDBe 1o04

X-ray diffraction
1.42Å resolution

Cys302Ser mutant of human mitochondrial aldehyde dehydrogenase complexed with NAD+ and Mg2+

Released:
Source organism: Homo sapiens
Primary publication:
Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase.
Biochemistry 42 7100-9 (2003)
PMID: 12795606

Function and Biology Details

Reaction catalysed:
An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldehyde dehydrogenase, mitochondrial Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 500 amino acids
Theoretical weight: 54.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P05091 (Residues: 18-517; Coverage: 97%)
Gene names: ALDH2, ALDM
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 141.211Å b: 152.487Å c: 177.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.145 0.171
Expression system: Escherichia coli BL21