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Magnesium in PDB 5r96: Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-AlphaEnzymatic activity of Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha
All present enzymatic activity of Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha:
2.7.11.24; Protein crystallography data
The structure of Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha, PDB code: 5r96
was solved by
G.F.De Nicola,
C.E.Nichols,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5r96:
The structure of Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha
(pdb code 5r96). 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 Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha, PDB code: 5r96: Magnesium binding site 1 out of 1 in 5r96Go back to Magnesium Binding Sites List in 5r96
Magnesium binding site 1 out
of 1 in the Pandda Analysis Group Deposition FORM1 Map Kinase P38-Alpha -- Fragment KCL095 in Complex with Map Kinase P38-Alpha
Mono view Stereo pair view
Reference:
C.Nichols,
J.Ng,
A.Keshu,
G.Kelly,
M.R.Conte,
M.S.Marber,
F.Fraternali,
G.F.De Nicola.
Mining the Pdb For Tractable Cases Where X-Ray Crystallography Combined with Fragment Screens Can Be Used to Systematically Design Protein-Protein Inhibitors: Two Test Cases Illustrated By IL1 Beta-IL1R and P38 Alpha-TAB1 Complexes. J.Med.Chem. V. 63 7559 2020.
Page generated: Mon Dec 14 21:08:20 2020
ISSN: ISSN 0022-2623 PubMed: 32543856 DOI: 10.1021/ACS.JMEDCHEM.0C00403 |
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