› 6c85

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb6c85/pdb
PDB entry 6c85 coloured by chain, front view.
PDB entry 6c85 coloured by chain, side view.
PDB entry 6c85 coloured by chain, top view.
Source organism: Blastomyces gilchristii SLH14081
Primary publication:
Structural insights into inhibitor binding to a fungal ortholog of aspartate semialdehyde dehydrogenase.
Dahal GP, Viola RE
Biochem Biophys Res Commun 503 2848-2854 (2018)
PMID: 30107909

Function and Biology Details

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-241456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PLQ 2 x PLQ
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-values:
R R work R free
0.202 0.2 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Molecular targets for antifungals in amino acid and protein biosynthetic pathways.
Kuplińska et al. (2021)

1 mention without citation

Structural characterization of aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa and Neisseria gonorrhoeae.
Teakel et al. (2022)