X-ray diffraction
2.4Å resolution

Crystal structure of aspartate semialdehyde dehydrogenase from Blastomyces dermatitidis with p-benzoquinone

Primary publication:
Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase.
Biochem. Biophys. Res. Commun. 503 2848-2854 (2018)
PMID: 30107909

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aspartate-semialdehyde dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 40.15 KDa
Source organism: Blastomyces gilchristii SLH14081
Expression system: Escherichia coli BL21(DE3)
  • Canonical: C5GC63 (Residues: 1-362; Coverage: 100%)
Gene name: BDCG_01946
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P3221
Unit cell:
a: 107.351Å b: 107.351Å c: 223.096Å
α: 90° β: 90° γ: 120°
R R work R free
0.202 0.2 0.241
Expression system: Escherichia coli BL21(DE3)