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Magnesium in PDB 6h8y: T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.Enzymatic activity of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.
All present enzymatic activity of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.:
5.4.2.6; Protein crystallography data
The structure of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A., PDB code: 6h8y
was solved by
A.J.Robertson,
C.Bisson,
J.P.Waltho,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6h8y:
The structure of T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A. also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.
(pdb code 6h8y). 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 T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A., PDB code: 6h8y: Magnesium binding site 1 out of 1 in 6h8yGo back to Magnesium Binding Sites List in 6h8y
Magnesium binding site 1 out
of 1 in the T16A Variant of Beta-Phosphoglucomutase From Lactococcus Lactis in An Open Conformer Complexed with Aluminium Tetrafluoride to 1.9 A.
Mono view Stereo pair view
Reference:
A.J.Robertson,
C.Bisson,
J.P.Waltho.
Transition State of Phospho-Enzyme Hydrolysis in Beta-Phosphoglucomutase. To Be Published.
Page generated: Mon Jan 25 08:44:12 2021
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