› 4oe5

X-ray diffraction
1.95Å resolution

Structure of Human ALDH4A1 Crystallized in Space Group P21

Released:
DOI: 10.2210/pdb4oe5/pdb
PDB entry 4oe5 coloured by chain, front view.
PDB entry 4oe5 coloured by chain, side view.
PDB entry 4oe5 coloured by chain, top view.
Source organism: Homo sapiens
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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 549 amino acids
Theoretical weight: 60.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30038 (Residues: 18-563; Coverage: 97%)
Gene names: ALDH4, ALDH4A1, P5CDH
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 91.96Å b: 121.335Å c: 93.397Å
α: 90° β: 104.23° γ: 90°
R-values:
R R work R free
0.196 0.194 0.235
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

4 mentions without citation

Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.
Luo et al. (2015)
3 more