› 1oza

X-ray diffraction
2.06Å resolution

Crystal Structure of the R103L Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae

Released:
DOI: 10.2210/pdb1oza/pdb
PDB entry 1oza coloured by chain, front view.
PDB entry 1oza coloured by chain, side view.
PDB entry 1oza coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE
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:
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: 40.54 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21212
Unit cell:
a: 112.651Å b: 53.878Å c: 55.071Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.208 0.243
Expression system: Escherichia coli BL21(DE3)

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Citations

10 citation in other articles

A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii.
Faehnle et al. (2005)
9 more

2 mentions without citation

The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding.
Bakan et al. (2009)
1 more