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Atomistry » Manganese » PDB 6rwz-6txf » 6s2u | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 6rwz-6txf » 6s2u » |
Manganese 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:
Manganese Binding Sites:
The binding sites of Manganese 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 Manganese atom.
In total only one binding site of Manganese was determined in the Structure of the Catalytic Domain of T. Thermophilus Rel in Complex with Amp and Ppgpp, PDB code: 6s2u: Manganese binding site 1 out of 1 in 6s2uGo back to Manganese Binding Sites List in 6s2u
Manganese binding site 1 out
of 1 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 05:00:40 2020
ISSN: ESSN 1552-4469 PubMed: 32393900 DOI: 10.1038/S41589-020-0520-2 |
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