› 2ono

X-ray diffraction
2.15Å resolution

Arg475Gln Mutant of Mitochondrial Aldehyde Dehydrogenase, apo form, pseudo-merohedrally twinned

Released:
DOI: 10.2210/pdb2ono/pdb
PDB entry 2ono coloured by chain, front view.
PDB entry 2ono coloured by chain, side view.
PDB entry 2ono coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487.
Larson HN, Zhou J, Chen Z, Stamler JS, Weiner H, Hurley TD
J Biol Chem 282 12940-50 (2007)
PMID: 17327228

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138420 (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: 54.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05091 (Residues: 18-517; Coverage: 97%)
Gene names: ALDH2, ALDM
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 101.472Å b: 175.85Å c: 101.458Å
α: 90° β: 94.79° γ: 90°
R-values:
R R work R free
0.251 not available 0.314
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily.
Marchitti et al. (2008)
17 more

1 mention without citation

Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487.
Larson et al. (2007)