› 4oe4

X-ray diffraction
2.17Å resolution

Crystal Structure of Yeast ALDH4A1 Complexed with NAD+

Released:
DOI: 10.2210/pdb4oe4/pdb
PDB entry 4oe4 coloured by chain, front view.
PDB entry 4oe4 coloured by chain, side view.
PDB entry 4oe4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state.
Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ
Biochemistry 53 1350-9 (2014)
PMID: 24502590

Function and Biology Details

Reaction catalysed: 
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139471 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 580 amino acids
Theoretical weight: 65.11 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P07275 (Residues: 23-575; Coverage: 96%)
Gene names: PUT2, YHR037W
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P63
Unit cell:
a: 108.037Å b: 108.037Å c: 181.027Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.173 0.212
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Role of Proline in Pathogen and Host Interactions.
Christgen et al. (2019)
3 more

1 mention without citation

Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state.
Pemberton et al. (2014)