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Calcium in PDB 6zma: Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 140 Bar of Krypton Using the Soak and Freeze MethodologyProtein crystallography data
The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 140 Bar of Krypton Using the Soak and Freeze Methodology, PDB code: 6zma
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 6zma:
The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 140 Bar of Krypton Using the Soak and Freeze Methodology 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 140 Bar of Krypton Using the Soak and Freeze Methodology
(pdb code 6zma). 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 140 Bar of Krypton Using the Soak and Freeze Methodology, PDB code: 6zma: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 6zmaGo back to Calcium Binding Sites List in 6zma
Calcium binding site 1 out
of 2 in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 140 Bar of Krypton Using the Soak and Freeze Methodology
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 6zmaGo back to Calcium Binding Sites List in 6zma
Calcium binding site 2 out
of 2 in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 140 Bar of Krypton Using the Soak and Freeze Methodology
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: Sat Dec 12 07:59:12 2020
ISSN: ESSN 1362-4962 PubMed: 32785618 DOI: 10.1093/NAR/GKAA667 |
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