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Atomistry » Zinc » PDB 5l0e-5lca » 5laq » |
Zinc 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:
Zinc Binding Sites:
The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Phosphodiesterase 4B Catalytic Domain with Inhibitor Npd-001, PDB code: 5laq: Zinc binding site 1 out of 1 in 5laqGo back to![]() ![]()
Zinc 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: Sun Oct 27 20:52:50 2024
ISSN: ISSN 1520-4804 PubMed: 29672041 DOI: 10.1021/ACS.JMEDCHEM.7B01670 |
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