› 4fr8

X-ray diffraction
2.2Å resolution

Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin

Released:
DOI: 10.2210/pdb4fr8/pdb
PDB entry 4fr8 coloured by chain, front view.
PDB entry 4fr8 coloured by chain, side view.
PDB entry 4fr8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Vascular bioactivation of nitroglycerin by aldehyde dehydrogenase-2: reaction intermediates revealed by crystallography and mass spectrometry.
Lang BS, Gorren AC, Oberdorfer G, Wenzl MV, Furdui CM, Poole LB, Mayer B, Gruber K
J Biol Chem 287 38124-34 (2012)
PMID: 22988236

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
UniProt:
  • Canonical: P05091 (Residues: 18-517; Coverage: 97%)
Gene names: ALDH2, ALDM
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
6 bound ligands:
Ligand TNG 1 x TNG
Ligand MG 8 x MG
Ligand URE 6 x URE
Ligand NA 8 x NA
Ligand ADP 4 x ADP
Ligand BTB 1 x BTB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 101.663Å b: 175.916Å c: 102.296Å
α: 90° β: 95.01° γ: 90°
R-values:
R R work R free
0.134 0.132 0.167
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Organic Nitrate Therapy, Nitrate Tolerance, and Nitrate-Induced Endothelial Dysfunction: Emphasis on Redox Biology and Oxidative Stress.
Daiber et al. (2015)
6 more

4 mentions without citation

Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway.
Jia et al. (2017)
3 more