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Magnesium in PDB 5laq: Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001Enzymatic activity of Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001
All present enzymatic activity of Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001:
3.1.4.53; Protein crystallography data
The structure of Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001, PDB code: 5laq
was solved by
A.K.Singh,
D.G.Brown,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5laq:
The structure of Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001
(pdb code 5laq). 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 Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001, PDB code: 5laq: Magnesium binding site 1 out of 1 in 5laqGo back to Magnesium Binding Sites List in 5laq
Magnesium binding site 1 out
of 1 in the Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001
Mono view Stereo pair view
Reference:
A.R.Blaazer,
A.K.Singh,
E.De Heuvel,
E.Edink,
K.M.Orrling,
J.J.N.Veerman,
T.Van Den Bergh,
C.Jansen,
E.Balasubramaniam,
W.J.Mooij,
H.Custers,
M.Sijm,
D.N.A.Tagoe,
T.D.Kalejaiye,
J.C.Munday,
H.Tenor,
A.Matheeussen,
M.Wijtmans,
M.Siderius,
C.De Graaf,
L.Maes,
H.P.De Koning,
D.S.Bailey,
G.J.Sterk,
I.J.P.De Esch,
D.G.Brown,
R.Leurs.
Targeting A Subpocket in Trypanosoma Brucei Phosphodiesterase B1 (TBRPDEB1) Enables the Structure-Based Discovery of Selective Inhibitors with Trypanocidal Activity. J. Med. Chem. V. 61 3870 2018.
Page generated: Mon Dec 14 20:45:58 2020
ISSN: ISSN 1520-4804 PubMed: 29672041 DOI: 10.1021/ACS.JMEDCHEM.7B01670 |
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