X-ray diffraction
1.81Å resolution

Evidence of Kinetic Cooperativity in dimeric Ketopantoate Reductase from Staphylococcus aureus


Function and Biology Details

Reactions catalysed:
(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH
6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2-dehydropantoate 2-reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.44 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
  • Canonical: A0A0J9X283 (Residues: 1-1, 3-286; Coverage: 97%)
Gene names: CH52_06005, DA92_02185
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand NDP 2 x NDP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 42.18Å b: 85.21Å c: 177.06Å
α: 90° β: 90° γ: 90°
R R work R free
0.174 0.173 0.211
Expression system: Escherichia coli