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Atomistry » Calcium » PDB 9odw-9uuu » 9udg | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 9odw-9uuu » 9udg » |
Calcium in PDB 9udg: Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42Enzymatic activity of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42
All present enzymatic activity of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42:
7.2.1.1; Other elements in 9udg:
The structure of Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42 also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42
(pdb code 9udg). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42, PDB code: 9udg: Calcium binding site 1 out of 1 in 9udgGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Cryo-Em Structure of Na+-Translocating Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae Reduced By Nadh, with Bound Aurachin D-42
![]() Mono view ![]() Stereo pair view
Reference:
M.Ishikawa-Fukuda,
T.Seki,
J.I.Kishikawa,
M.Takahiro,
K.I.Okazaki,
T.Kato,
B.Barquera,
H.Miyoshi,
M.Murai.
The Na + -Pumping Mechanism Driven By Redox Reactions in the Nadh-Quinone Oxidoreductase From Vibrio Cholerae Relies on Dynamic Conformational Changes. Biorxiv 2025.
Page generated: Thu Jul 10 10:27:41 2025
ISSN: ISSN 2692-8205 PubMed: 40501732 DOI: 10.1101/2025.06.01.656757 |
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