› 1ofn

X-ray diffraction
1.5Å resolution

Purification, crystallisation and preliminary structural studies of dTDP-4-keto-6-deoxy-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis; the fourth enzyme in the dTDP-L-epivancosamine biosynthetic pathway.

Released:
DOI: 10.2210/pdb1ofn/pdb
PDB entry 1ofn coloured by chain, front view.
PDB entry 1ofn coloured by chain, side view.
PDB entry 1ofn coloured by chain, top view.
Source organism: Amycolatopsis orientalis
Primary publication:
Purification, crystallization and preliminary structural studies of dTDP-4-keto-6-deoxy-glucose-5-epimerase (EvaD) from Amycolatopsis orientalis, the fourth enzyme in the dTDP-L-epivancosamine biosynthetic pathway.
Merkel AB, Temple GK, Burkart MD, Losey HC, Beis K, Walsh CT, Naismith JH
Acta Crystallogr D Biol Crystallogr 58 1226-8 (2002)
PMID: 12077451

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129416 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PCZA361.16 Chains: A, B
Molecule details ›
Chains: A, B
Length: 205 amino acids
Theoretical weight: 22.51 KDa
Source organism: Amycolatopsis orientalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O52806 (Residues: 1-205; Coverage: 100%)
Sequence domains: dTDP-4-dehydrorhamnose 3,5-epimerase
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 98.575Å b: 71.996Å c: 57.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.144 0.178
Expression system: Escherichia coli BL21(DE3)

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Citations

3 citation in other articles

Structure-based phylogeny as a diagnostic for functional characterization of proteins with a cupin fold.
Agarwal et al. (2009)
2 more

2 mentions without citation

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