1ps8

X-ray diffraction
2.4Å resolution

Crystal Structure of the R270K Mutant of Aspartate Semialdehyde dehydrogenase from Haemophilus influenzae

Released:
Source organism: Haemophilus influenzae
Primary publication:
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
Acta Crystallogr D Biol Crystallogr 60 1388-95 (2004)
PMID: 15272161

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-155209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 40.56 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P44801 (Residues: 1-371; Coverage: 100%)
Gene names: HI_0646, asd
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 113.883Å b: 54.624Å c: 57.119Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.285
Expression system: Escherichia coli BL21