› 1nx6

X-ray diffraction
2.15Å resolution

Crystal Structure of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae as a Tetrahedral Hemithiocetal Reaction intermediate with Phosphate at 2.15 A

Released:
DOI: 10.2210/pdb1nx6/pdb
PDB entry 1nx6 coloured by chain, front view.
PDB entry 1nx6 coloured by chain, side view.
PDB entry 1nx6 coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase.
Blanco J, Moore RA, Viola RE
Proc Natl Acad Sci U S A 100 12613-7 (2003)
PMID: 14559965

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 domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
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: 40.7 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P44801 (Residues: 1-371; Coverage: 100%)
Gene names: HI_0646, asd
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
1 modified residue:
Ligand HTI 1 x HTI

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21212
Unit cell:
a: 113.748Å b: 54.853Å c: 57.691Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.254 0.228 0.284
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Inhibition of lysine biosynthesis: an evolving antibiotic strategy.
Hutton et al. (2007)
23 other articles

6 mentions without citation

Arsenate replacing phosphate: alternative life chemistries and ion promiscuity.
Tawfik et al. (2011)
5 more