› 3rbv

X-ray diffraction
1.9Å resolution

Crystal Structure of KijD10, a 3-ketoreductase from Actinomadura kijaniata incomplex with NADP

Released:
DOI: 10.2210/pdb3rbv/pdb
PDB entry 3rbv coloured by chain, front view.
PDB entry 3rbv coloured by chain, side view.
PDB entry 3rbv coloured by chain, top view.
Source organism: Actinomadura kijaniata
Primary publication:
Combined structural and functional investigation of a C-3''-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose.
Kubiak RL, Holden HM
Biochemistry 50 5905-17 (2011)
PMID: 21598943

Function and Biology Details

Reaction catalysed: 
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 39.26 KDa
Source organism: Actinomadura kijaniata
Expression system: Escherichia coli
UniProt:
  • Canonical: B3TMR8 (Residues: 1-332; Coverage: 100%)
Gene name: KijD10
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
4 bound ligands:
Ligand EDO 1 x EDO
Ligand CL 2 x CL
Ligand NA 1 x NA
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 73.253Å b: 104.032Å c: 144.596Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.228
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
1 more

1 mention without citation

Structural and functional features of the NAD(P) dependent Gfo/Idh/MocA protein family oxidoreductases.
Taberman et al. (2016)