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Magnesium in PDB 6s2u: Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and PpgppEnzymatic activity of Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp
All present enzymatic activity of Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp:
2.7.6.5; Protein crystallography data
The structure of Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp, PDB code: 6s2u
was solved by
A.Garcia-Pino,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6s2u:
The structure of Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp
(pdb code 6s2u). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp, PDB code: 6s2u: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6s2uGo back to Magnesium Binding Sites List in 6s2u
Magnesium binding site 1 out
of 2 in the Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6s2uGo back to Magnesium Binding Sites List in 6s2u
Magnesium binding site 2 out
of 2 in the Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp
Mono view Stereo pair view
Reference:
H.Tamman,
K.Van Nerom,
H.Takada,
N.Vandenberk,
D.Scholl,
Y.Polikanov,
J.Hofkens,
A.Talavera,
V.Hauryliuk,
J.Hendrix,
A.Garcia-Pino.
A Nucleotide-Switch Mechanism Mediates Opposing Catalytic Activities of Rel Enzymes. Nat.Chem.Biol. V. 16 834 2020.
Page generated: Tue Dec 15 00:02:55 2020
ISSN: ESSN 1552-4469 PubMed: 32393900 DOI: 10.1038/S41589-020-0520-2 |
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