› 1epz

X-ray diffraction
1.75Å resolution

CRYSTAL STRUCTURE OF DTDP-6-DEOXY-D-XYLO-4-HEXULOASE 3,5-EPIMERASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM WITH BOUND LIGAND.

Released:
DOI: 10.2210/pdb1epz/pdb
PDB entry 1epz coloured by chain, front view.
PDB entry 1epz coloured by chain, side view.
PDB entry 1epz coloured by chain, top view.
Source organism: Methanothermobacter thermautotrophicus
Primary publication:
Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP.
Christendat D, Saridakis V, Dharamsi A, Bochkarev A, Pai EF, Arrowsmith CH, Edwards AM
J Biol Chem 275 24608-12 (2000)
PMID: 10827167

Function and Biology Details

Reaction catalysed: 
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
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-127917 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTDP-4-dehydrorhamnose 3,5-epimerase Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 21.7 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O27818 (Residues: 1-185; Coverage: 100%)
Gene names: MTH_1790, rmlC
Sequence domains: dTDP-4-dehydrorhamnose 3,5-epimerase
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
Ligand TYD 1 x TYD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 68.156Å b: 53.486Å c: 51.462Å
α: 90° β: 97.22° γ: 90°
R-values:
R R work R free
0.196 0.196 0.225
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Natural-product sugar biosynthesis and enzymatic glycodiversification.
Thibodeaux et al. (2008)
2 more

1 mention without citation

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