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Atomistry » Potassium » PDB 5mrm-5s9l » 5ncq | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 5mrm-5s9l » 5ncq » |
Potassium in PDB 5ncq: Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-AtpEnzymatic activity of Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp
All present enzymatic activity of Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp:
3.6.3.8; Protein crystallography data
The structure of Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp, PDB code: 5ncq
was solved by
M.Bublitz,
L.Kjellerup,
K.O'hanlon Cohrt,
S.Gordon,
A.L.Mortensen,
J.D.Clausen,
D.Pallin,
J.B.Hansen,
W.D.Brown,
A.Fuglsang,
A.-M.L.Winther,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ncq:
The structure of Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp
(pdb code 5ncq). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp, PDB code: 5ncq: Potassium binding site 1 out of 1 in 5ncqGo back to![]() ![]()
Potassium binding site 1 out
of 1 in the Structure of the (Sr) CA2+-Atpase Bound to A Tetrahydrocarbazole and Tnp-Atp
![]() Mono view ![]() Stereo pair view
Reference:
M.Bublitz,
L.Kjellerup,
K.O.Cohrt,
S.Gordon,
A.L.Mortensen,
J.D.Clausen,
T.D.Pallin,
J.B.Hansen,
A.T.Fuglsang,
W.Dalby-Brown,
A.L.Winther.
Tetrahydrocarbazoles Are A Novel Class of Potent P-Type Atpase Inhibitors with Antifungal Activity. Plos One V. 13 88620 2018.
Page generated: Mon Aug 12 14:19:10 2024
ISSN: ESSN 1932-6203 PubMed: 29293507 DOI: 10.1371/JOURNAL.PONE.0188620 |
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