› 3iwk

X-ray diffraction
2.4Å resolution

Crystal structure of aminoaldehyde dehydrogenase 1 from Pisum sativum (PsAMADH1)

Released:
DOI: 10.2210/pdb3iwk/pdb
PDB entry 3iwk coloured by chain, front view.
PDB entry 3iwk coloured by chain, side view.
PDB entry 3iwk coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
Tylichová M, Kopecný D, Moréra S, Briozzo P, Lenobel R, Snégaroff J, Sebela M
J Mol Biol 396 870-82 (2010)
PMID: 20026072

Function and Biology Details

Reactions catalysed: 
4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH
4-guanidinobutanal + NAD(+) + H(2)O = 4-guanidinobutanoate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186634 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoaldehyde dehydrogenase 1, peroxisomal Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 503 amino acids
Theoretical weight: 54.87 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VWZ1 (Residues: 1-503; Coverage: 100%)
Gene name: AMADH1
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 12 x NAD
3 bound ligands:
Ligand NA 12 x NA
Ligand GOL 19 x GOL
Ligand MRD 1 x MRD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 86.41Å b: 216.87Å c: 205.76Å
α: 90° β: 98.02° γ: 90°
R-values:
R R work R free
0.202 0.2 0.244
Expression system: Escherichia coli

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Citations

1 review citation

Polyamine-Derived Aminoaldehydes and Acrolein: Cytotoxicity, Reactivity and Analysis of the Induced Protein Modifications.
Šebela et al. (2023)
27 other articles

4 mentions without citation

Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus.
Halavaty et al. (2015)
3 more