X-ray diffraction
1.32Å resolution

Crystal Structure of Hyperthermophilic Thermotoga maritima L-Ketose-3-Epimerase with Co2+


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
5-keto-L-gluconate epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 290 amino acids
Theoretical weight: 32.68 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9WYP7 (Residues: 1-270; Coverage: 100%)
Gene names: TM_0416, iolO
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P1
Unit cell:
a: 50.284Å b: 55.255Å c: 58.754Å
α: 107.14° β: 102.35° γ: 92.2°
R R work R free
0.172 0.171 0.189
Expression system: Escherichia coli BL21(DE3)