› 1mzr

X-ray diffraction
2.13Å resolution

Structure of dkga from E.coli at 2.13 A resolution solved by molecular replacement

Released:
DOI: 10.2210/pdb1mzr/pdb
PDB entry 1mzr coloured by chain, front view.
PDB entry 1mzr coloured by chain, side view.
PDB entry 1mzr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of Escherichia coli DkgA, a broad-specificity aldo-keto reductase.
Jeudy S, Monchois V, Maza C, Claverie JM, Abergel C
Proteins 62 302-7 (2006)
PMID: 16284956

Function and Biology Details

Reaction catalysed: 
2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,5-diketo-D-gluconic acid reductase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 33.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q46857 (Residues: 2-275; Coverage: 100%)
Gene names: JW5499, b3012, dkgA, yqhE
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

2 bound ligands:
Ligand PO4 5 x PO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 139.177Å b: 145.697Å c: 79.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.22
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Gates of enzymes.
Gora et al. (2013)
10 other articles

8 mentions without citation

Targeting aberrant glutathione metabolism to eradicate human acute myelogenous leukemia cells.
Pei et al. (2013)
7 more