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Atomistry » Zinc » PDB 5g2b-5gk8 » 5g2b » |
Zinc in PDB 5g2b: Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008Protein crystallography data
The structure of Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008, PDB code: 5g2b
was solved by
A.K.Singh,
E.S.Anthonyrajah,
D.G.Brown,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5g2b:
The structure of Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008
(pdb code 5g2b). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008, PDB code: 5g2b: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5g2bGo back to Zinc Binding Sites List in 5g2b
Zinc binding site 1 out
of 2 in the Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5g2bGo back to Zinc Binding Sites List in 5g2b
Zinc binding site 2 out
of 2 in the Crystal Structure of T. Brucei Pde-B1 Catalytic Domain with Inhibitor Npd-008
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 16:53:54 2024
ISSN: ISSN 1520-4804 PubMed: 29672041 DOI: 10.1021/ACS.JMEDCHEM.7B01670 |
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