› 3q0e

X-ray diffraction
1.8Å resolution

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Vibrio Cholerae with product of S-allyl-L-cysteine sulfoxide

Released:
DOI: 10.2210/pdb3q0e/pdb
PDB entry 3q0e coloured by chain, front view.
PDB entry 3q0e coloured by chain, side view.
PDB entry 3q0e coloured by chain, top view.
Source organism: Vibrio cholerae
Primary publication:
Structural characterization of inhibitors with selectivity against members of a homologous enzyme family.
Pavlovsky AG, Liu X, Faehnle CR, Potente N, Viola RE
Chem Biol Drug Des 79 128-36 (2012)
PMID: 22039970

Function and Biology Details

Reaction catalysed: 
L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 40.54 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KQG2 (Residues: 1-370; Coverage: 100%)
Gene names: VC_2036, asd1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CYS 2 x CYS
Ligand SO4 2 x SO4
Ligand ACT 1 x ACT
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 107.648Å b: 107.648Å c: 153.953Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.206
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Cysteamine revisited: repair of arginine to cysteine mutations.
Gallego-Villar et al. (2017)
1 more

2 mentions without citation

Structural characterization of inhibitors with selectivity against members of a homologous enzyme family.
Pavlovsky et al. (2012)
1 more