› 6d97

X-ray diffraction
2.2Å resolution

Structure of aldehyde dehydrogenase 12 (ALDH12) from Zea mays

Released:
DOI: 10.2210/pdb6d97/pdb
PDB 6d97 coloured by chain and viewed from the front.
PDB 6d97 coloured by chain and viewed from the side.
PDB 6d97 coloured by chain and viewed from the top.
Source organism: Zea mays
Primary publication:
Structural and Biochemical Characterization of Aldehyde Dehydrogenase 12, the Last Enzyme of Proline Catabolism in Plants.
Korasick DA, Končitíková R, Kopečná M, Hájková E, Vigouroux A, Moréra S, Becker DF, Šebela M, Tanner JJ, Kopečný D
J. Mol. Biol. (2018)
PMID: 30580036

Function and Biology Details

Reaction catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldedh domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 547 amino acids
Theoretical weight: 60.47 KDa
Source organism: Zea mays
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A2H4PMI3 (Residues: 17-549; Coverage: 97%)
Gene name: ALDH12
Sequence domains: Aldehyde dehydrogenase family

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 160.642Å b: 123.737Å c: 103.707Å
α: 90° β: 105.62° γ: 90°
R-values:
R R work R free
0.167 0.165 0.21
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Recent Development on Plant Aldehyde Dehydrogenase Enzymes and Their Functions in Plant Development and Stress Signaling.
Tola et al. (2020)
1 other article