› 1pqp

X-ray diffraction
2.06Å resolution

Crystal Structure of the C136S Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae Bound with Aspartate Semialdehyde and Phosphate

Released:
DOI: 10.2210/pdb1pqp/pdb
PDB entry 1pqp coloured by chain, front view.
PDB entry 1pqp coloured by chain, side view.
PDB entry 1pqp coloured by chain, top view.
Source organism: Haemophilus influenzae Rd KW20
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

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 40.57 KDa
Source organism: Haemophilus influenzae Rd KW20
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

2 bound ligands:
Ligand PO4 1 x PO4
Ligand HSE 1 x HSE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 113.949Å b: 55.059Å c: 57.832Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.228 0.286
Expression system: Escherichia coli BL21

Quick links

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

1 mention without citation

The catalytic machinery of a key enzyme in amino Acid biosynthesis.
Viola et al. (2011)