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Calcium in PDB 7xk5: Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3
Enzymatic activity of Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3
All present enzymatic activity of Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3:
7.2.1.1;
7.2.1.1;
Other elements in 7xk5:
The structure of Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3 also contains other interesting chemical elements:
| Iron | (Fe) | 4 atoms |
Calcium Binding Sites:
The binding sites of Calcium atom in the Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3
(pdb code 7xk5). 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+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3, PDB code: 7xk5:
In total only one binding site of Calcium was determined in the Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3, PDB code: 7xk5:
Calcium binding site 1 out of 1 in 7xk5
Go back to
Calcium Binding Sites List in 7xk5
Calcium binding site 1 out
of 1 in the Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3
Mono view
Stereo pair view
Mono view
Stereo pair view
| A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cryo-Em Structure of Na+-Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae, State 3 within 5.0Å range: |
Reference:
J.I.Kishikawa,
M.Ishikawa,
T.Masuya,
M.Murai,
Y.Kitazumi,
N.L.Butler,
T.Kato,
B.Barquera,
H.Miyoshi.
Cryo-Em Structures of Na + -Pumping Nadh-Ubiquinone Oxidoreductase From Vibrio Cholerae. Nat Commun V. 13 4082 2022.
ISSN: ESSN 2041-1723
PubMed: 35882843
DOI: 10.1038/S41467-022-31718-1
Page generated: Thu Jul 10 02:27:44 2025
ISSN: ESSN 2041-1723
PubMed: 35882843
DOI: 10.1038/S41467-022-31718-1
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