› 4lh0

X-ray diffraction
1.67Å resolution

Structure of mouse 1-Pyrroline-5-Carboxylate Dehydrogenase (ALDH4A1) complexed with glyoxylate

Released:
DOI: 10.2210/pdb4lh0/pdb
PDB entry 4lh0 coloured by chain, front view.
PDB entry 4lh0 coloured by chain, side view.
PDB entry 4lh0 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural basis of substrate selectivity of Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length.
Pemberton TA, Tanner JJ
Arch Biochem Biophys 538 34-40 (2013)
PMID: 23928095

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 563 amino acids
Theoretical weight: 61.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8CHT0 (Residues: 21-562; Coverage: 96%)
Gene name: Aldh4a1
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GLV 3 x GLV
Ligand 1PE 2 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 84.87Å b: 94.242Å c: 132.087Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.184
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structure, function, and mechanism of proline utilization A (PutA).
Liu et al. (2017)
1 more

1 mention without citation

Structural basis of substrate selectivity of Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length.
Pemberton et al. (2013)