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Atomistry » Magnesium » PDB 3ktv-3l8z » 3l0y | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3ktv-3l8z » 3l0y » |
Magnesium in PDB 3l0y: Crystal Structure of SCP1 Phosphatase D98A MutantEnzymatic activity of Crystal Structure of SCP1 Phosphatase D98A Mutant
All present enzymatic activity of Crystal Structure of SCP1 Phosphatase D98A Mutant:
3.1.3.16; Protein crystallography data
The structure of Crystal Structure of SCP1 Phosphatase D98A Mutant, PDB code: 3l0y
was solved by
M.Zhang,
Y.Zhang,
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 Crystal Structure of SCP1 Phosphatase D98A Mutant
(pdb code 3l0y). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of SCP1 Phosphatase D98A Mutant, PDB code: 3l0y: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3l0yGo back to Magnesium Binding Sites List in 3l0y
Magnesium binding site 1 out
of 2 in the Crystal Structure of SCP1 Phosphatase D98A Mutant
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3l0yGo back to Magnesium Binding Sites List in 3l0y
Magnesium binding site 2 out
of 2 in the Crystal Structure of SCP1 Phosphatase D98A Mutant
Mono view Stereo pair view
Reference:
M.Zhang,
J.Liu,
Y.Kim,
J.E.Dixon,
S.L.Pfaff,
G.N.Gill,
J.P.Noel,
Y.Zhang.
Structural and Functional Analysis of the Phosphoryl Transfer Reaction Mediated By the Human Small C-Terminal Domain Phosphatase, SCP1. Protein Sci. V. 19 974 2010.
Page generated: Mon Dec 14 08:23:36 2020
ISSN: ISSN 0961-8368 PubMed: 20222012 DOI: 10.1002/PRO.375 |
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