› 1m9h

X-ray diffraction
2Å resolution

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

Released:
DOI: 10.2210/pdb1m9h/pdb
PDB 1m9h coloured by chain and viewed from the front.
PDB 1m9h coloured by chain and viewed from the side.
PDB 1m9h coloured by chain and viewed from the top.
Source organism: Corynebacterium sp.
Primary publication:
Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase.
Sanli G, Banta S, Anderson S, Blaber M
Protein Sci. 13 504-12 (2004)
PMID: 14718658

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,5-diketo-D-gluconic acid reductase A Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 30.06 KDa
Source organism: Corynebacterium sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P06632 (Residues: 1-278; Coverage: 100%)
Gene name: dkgA
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 111.95Å b: 55.24Å c: 51.54Å
α: 90° β: 111.66° γ: 90°
R-values:
R R work R free
0.214 0.213 0.261
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Extreme makeover: Engineering the activity of a thermostable alcohol dehydrogenase (AdhD) from Pyrococcus furiosus.
Solanki et al. (2016)
12 other articles

2 mentions without citation

Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies.
Di Luccio et al. (2006)
1 more