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Atomistry » Magnesium » PDB 3zi8-3zwk » 3zu6 » |
Magnesium in PDB 3zu6: The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products.Enzymatic activity of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products.
All present enzymatic activity of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products.:
3.1.3.70; Protein crystallography data
The structure of The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products., PDB code: 3zu6
was solved by
S.Goncalves,
N.Borges,
A.M.Esteves,
H.Santos,
P.M.Matias,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products.
(pdb code 3zu6). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products., PDB code: 3zu6: Magnesium binding site 1 out of 1 in 3zu6Go back to Magnesium Binding Sites List in 3zu6
Magnesium binding site 1 out
of 1 in the The 3-Dimensional Structure of Mpgp From Thermus Thermophilus HB27, in Complex with the Alpha-Mannosylglycerate and Orthophosphate Reaction Products.
Mono view Stereo pair view
Reference:
S.Goncalves,
A.M.Esteves,
H.Santos,
N.Borges,
P.M.Matias.
The Three-Dimensional Structure of Mannosyl-3- Phosphoglycerate Phosphatase From Thermus Thermophilus HB27: A New Member of the Haloalkanoic Acid Dehalogenase Superfamily. Biochemistry V. 50 9551 2011.
Page generated: Mon Dec 14 09:04:29 2020
ISSN: ISSN 0006-2960 PubMed: 21961705 DOI: 10.1021/BI201171H |
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