› 2gyy

X-ray diffraction
2.1Å resolution

Structure of aspartate semialdehyde dehydrogenase (ASADH) from Streptococcus pneumoniae

Released:
DOI: 10.2210/pdb2gyy/pdb
PDB entry 2gyy coloured by chain, front view.
PDB entry 2gyy coloured by chain, side view.
PDB entry 2gyy coloured by chain, top view.
Source organism: Streptococcus pneumoniae
Primary publication:
Examination of key intermediates in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase from a gram-positive infectious bacteria.
Faehnle CR, Le Coq J, Liu X, Viola RE
J Biol Chem 281 31031-40 (2006)
PMID: 16895909

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-101434 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 366 amino acids
Theoretical weight: 40.04 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2UPS5 (Residues: 1-358; Coverage: 100%)
Gene names: SP_1013, asd
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 72.479Å b: 78.686Å c: 243.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.221
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

3 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
2 more