› 4oe6

X-ray diffraction
1.95Å resolution

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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P63
Unit cell:
a: 109.032Å b: 109.032Å c: 181.246Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.177 0.202
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

5 mentions without citation

Insights into Aldehyde Dehydrogenase Enzymes: A Structural Perspective.
Shortall et al. (2021)
4 more