4s3m

X-ray diffraction
2.6Å resolution

Evidence of kinetic cooperativity in dimeric Ketopantoate Reductase from Staphylococcus aureus

Released:
Entry authors: Sanchez JE, Walsh Jr RM, Wood ZA

Function and Biology Details

Reaction catalysed:
6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphogluconate dehydrogenase, decarboxylating Chains: A, B
Molecule details ›
Chains: A, B
Length: 294 amino acids
Theoretical weight: 33.48 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0J9X201 (Residues: 3-286; Coverage: 97%)
Gene name: SAV2600
Sequence domains:
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Unit cell:
a: 88.648Å b: 66.764Å c: 122.378Å
α: 90° β: 110.15° γ: 90°
R-values:
R R work R free
0.227 0.222 0.268
Expression system: Escherichia coli