X-ray diffraction
1.8Å resolution

The 3-dimensional structure of MpgP from Thermus thermophilus HB27, in complex with the alpha-mannosylglycerate and orthophosphate reaction products.

Source organism: Thermus thermophilus HB27
Entry authors: Goncalves S, Esteves AM, Santos H, Borges N, Matias PM

Function and Biology Details

Reaction catalysed:
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H(2)O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Mannosyl-3-phosphoglycerate phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 28.22 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q72K29 (Residues: 1-259; Coverage: 100%)
Gene name: TT_C0589
Sequence domains: haloacid dehalogenase-like hydrolase
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 39.368Å b: 88.049Å c: 146.457Å
α: 90° β: 90° γ: 90°
R R work R free
0.183 0.18 0.23
Expression system: Escherichia coli BL21(DE3)