› 2hk0

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
D-psicose = D-fructose
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108863 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-psicose 3-epimerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 309 amino acids
Theoretical weight: 34.21 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: A9CH28 (Residues: 1-289; Coverage: 100%)
Gene names: Atu4750, dpe
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 28 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 102.4Å b: 113Å c: 131.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.233
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Recent advances on applications and biotechnological production of D-psicose.
Mu et al. (2012)
7 more

7 mentions without citation

Research Advances of d-allulose: An Overview of Physiological Functions, Enzymatic Biotransformation Technologies, and Production Processes.
Xia et al. (2021)
6 more