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Atomistry » Calcium » PDB 6ywn-6zqr » 6zmc » |
Calcium in PDB 6zmc: Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing MethodProtein crystallography data
The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method, PDB code: 6zmc
was solved by
P.Carpentier,
M.Atta,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6zmc:
The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method
(pdb code 6zmc). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method, PDB code: 6zmc: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 6zmcGo back to Calcium Binding Sites List in 6zmc
Calcium binding site 1 out
of 2 in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 6zmcGo back to Calcium Binding Sites List in 6zmc
Calcium binding site 2 out
of 2 in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method
Mono view Stereo pair view
Reference:
P.Carpentier,
C.Lepretre,
C.Basset,
T.Douki,
S.Torelli,
V.Duarte,
D.Hamdane,
M.Fontecave,
M.Atta.
Structural, Biochemical and Functional Analyses of Trna-Monooxygenase Enzyme Miae From Pseudomonas Putida Provide Insights Into Trna/Miae Interaction. Nucleic Acids Res. V. 48 9918 2020.
Page generated: Thu Jul 18 22:44:04 2024
ISSN: ESSN 1362-4962 PubMed: 32785618 DOI: 10.1093/NAR/GKAA667 |
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