X-ray diffraction
2.3Å resolution

The crystal structure of human C340A SSADH

Source organism: Homo sapiens
Primary publication:
Redox-switch modulation of human SSADH by dynamic catalytic loop.
EMBO J. 28 959-68 (2009)
PMID: 19300440

Function and Biology Details

Reaction catalysed:
Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dodecamer
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Succinate-semialdehyde dehydrogenase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 52.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P51649 (Residues: 49-535; Coverage: 91%)
Gene names: ALDH5A1, SSADH
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: F432
Unit cell:
a: 265.895Å b: 265.895Å c: 265.895Å
α: 90° β: 90° γ: 90°
R R work R free
0.229 0.229 0.264
Expression system: Escherichia coli