› 3jz4

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
Succinate semialdehyde + NADP(+) + H(2)O = succinate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Succinate-semialdehyde dehydrogenase [NADP(+)] GabD Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 481 amino acids
Theoretical weight: 51.68 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25526 (Residues: 2-482; Coverage: 100%)
Gene names: JW2636, b2661, gabD
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P4212
Unit cell:
a: 151.885Å b: 151.885Å c: 165.772Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Succinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance.
Kim et al. (2011)
12 other articles

9 mentions without citation

The X-ray crystal structure of Escherichia coli succinic semialdehyde dehydrogenase; structural insights into NADP+/enzyme interactions.
Langendorf et al. (2010)
8 more