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Magnesium in PDB 5w2h: Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and AdpEnzymatic activity of Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp
All present enzymatic activity of Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp:
2.7.1.151; Protein crystallography data
The structure of Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp, PDB code: 5w2h
was solved by
H.Wang,
S.B.Shears,
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 the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp
(pdb code 5w2h). 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 the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp, PDB code: 5w2h: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 5w2hGo back to Magnesium Binding Sites List in 5w2h
Magnesium binding site 1 out
of 2 in the Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 5w2hGo back to Magnesium Binding Sites List in 5w2h
Magnesium binding site 2 out
of 2 in the Crystal Structure of the Core Catalytic Domain of Human Inositol Phosphate Multikinase in Complex with Ins(1,4,5)P3 and Adp
Mono view Stereo pair view
Reference:
H.Wang,
S.B.Shears.
Structural Features of Human Inositol Phosphate Multikinase Rationalize Its Inositol Phosphate Kinase and Phosphoinositide 3-Kinase Activities. J. Biol. Chem. V. 292 18192 2017.
Page generated: Mon Dec 14 21:20:13 2020
ISSN: ESSN 1083-351X PubMed: 28882892 DOI: 10.1074/JBC.M117.801845 |
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