› 4o9g

X-ray diffraction
1.9Å resolution

Crystal structure of the H51N mutant of the 3,4-ketoisomerase QdtA from Thermoanaerobacterium thermosaccharolyticum in complex with TDP-4-keto-6-deoxyglucose

Released:
DOI: 10.2210/pdb4o9g/pdb
PDB entry 4o9g coloured by chain, front view.
PDB entry 4o9g coloured by chain, side view.
PDB entry 4o9g coloured by chain, top view.
Source organism: Thermoanaerobacterium thermosaccharolyticum
Primary publication:
The molecular architecture of QdtA, a sugar 3,4-ketoisomerase from Thermoanaerobacterium thermosaccharolyticum.
Thoden JB, Holden HM
Protein Sci 23 683-92 (2014)
PMID: 24616215

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180371 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sugar 3,4-ketoisomerase QdtA cupin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 17.14 KDa
Source organism: Thermoanaerobacterium thermosaccharolyticum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6TFC5 (Residues: 1-136; Coverage: 100%)
Gene name: qdtA
Sequence domains: WxcM-like, C-terminal
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand T46 2 x T46
Ligand EDO 1 x EDO
Ligand 4TD 1 x 4TD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P4212
Unit cell:
a: 95.396Å b: 95.396Å c: 94.643Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.241
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Characterization of the dTDP-Fuc3N and dTDP-Qui3N biosynthetic pathways in Campylobacter jejuni 81116.
Li et al. (2017)

3 mentions without citation

Bacterial Sugar 3,4-Ketoisomerases: Structural Insight into Product Stereochemistry.
Thoden et al. (2015)
2 more