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Atomistry » Copper » PDB 9csu-9j9q » 9e7h | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Copper » PDB 9csu-9j9q » 9e7h » |
Copper in PDB 9e7h: Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex DatasetEnzymatic activity of Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset
All present enzymatic activity of Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset:
1.3.7.7; Other elements in 9e7h:
The structure of Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset
(pdb code 9e7h). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset, PDB code: 9e7h: Jump to Copper binding site number: 1; 2; Copper binding site 1 out of 2 in 9e7hGo back to![]() ![]()
Copper binding site 1 out
of 2 in the Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset
![]() Mono view ![]() Stereo pair view
Copper binding site 2 out of 2 in 9e7hGo back to![]() ![]()
Copper binding site 2 out
of 2 in the Cryoem Structure of Bchn-Bchb Bound to Pchlide From the Dpor Under Turnover Complex Dataset
![]() Mono view ![]() Stereo pair view
Reference:
R.Kashyap,
N.Walsh,
J.Deveryshetty,
M.Tokmina-Lukaszewska,
K.Zhao,
Y.J.Gan,
B.M.Hoffman,
R.Sarangi,
B.Bothner,
B.Bennett,
E.Antony.
Cryo-Em Captures the Coordination of Asymmetric Electron Transfer Through A Di-Copper Site in Dpor. Nat Commun V. 16 3866 2025.
Page generated: Mon Jul 14 09:52:20 2025
ISSN: ESSN 2041-1723 PubMed: 40274796 DOI: 10.1038/S41467-025-59158-7 |
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