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Magnesium in PDB 8a1z: Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-HydroxyureaEnzymatic activity of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea
All present enzymatic activity of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea:
3.1.3.3; Protein crystallography data
The structure of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea, PDB code: 8a1z
was solved by
M.Haufroid,
J.Wouters,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8a1z:
The structure of Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea
(pdb code 8a1z). 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 Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea, PDB code: 8a1z: Magnesium binding site 1 out of 1 in 8a1zGo back to Magnesium Binding Sites List in 8a1z
Magnesium binding site 1 out
of 1 in the Crystal Structure of Phosphoserine Phosphatase Serb From Mycobacterium Avium in Complex with 1-(2,4-Dichlorophenyl)-3-Hydroxyurea
Mono view Stereo pair view
Reference:
M.Haufroid,
A.N.Volkov,
J.Wouters.
Targeting the Phosphoserine Phosphatase MTSERB2 For Tuberculosis Drug Discovery, An Hybrid Knowledge Based /Fragment Based Approach. Eur.J.Med.Chem. V. 245 14935 2022.
Page generated: Fri Apr 7 05:03:45 2023
ISSN: ISSN 0223-5234 PubMed: 36403421 DOI: 10.1016/J.EJMECH.2022.114935 |
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