3v9h

X-ray diffraction
2.4Å resolution

Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352A

Released:
Source organism: Homo sapiens

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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: 566 amino acids
Theoretical weight: 62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30038 (Residues: 18-563; Coverage: 97%)
  • Best match: P30038-2 (Residues: 1-503)
Gene names: ALDH4, ALDH4A1, P5CDH
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P65
Unit cell:
a: 149.131Å b: 149.131Å c: 190.687Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.21 0.251
Expression system: Escherichia coli BL21(DE3)