› 4yca

X-ray diffraction
1.81Å resolution

Evidence of Kinetic Cooperativity in dimeric Ketopantoate Reductase from Staphylococcus aureus

Released:
DOI: 10.2210/pdb4yca/pdb
PDB entry 4yca coloured by chain, front view.
PDB entry 4yca coloured by chain, side view.
PDB entry 4yca coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus.
Sanchez JE, Gross PG, Goetze RW, Walsh RM, Peeples WB, Wood ZA
Biochemistry 54 3360-3369 (2015)
PMID: 25946571

Function and Biology Details

Reaction catalysed: 
(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.174 0.173 0.211
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species.
Daczkowski et al. (2017)
6 more

1 mention without citation

Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus.
Sanchez et al. (2015)