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Atomistry » Magnesium » PDB 7qbm-7qpi » 7qoc » |
Magnesium in PDB 7qoc: Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium GlutamicumEnzymatic activity of Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum
All present enzymatic activity of Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum:
3.1.7.2; Protein crystallography data
The structure of Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum, PDB code: 7qoc
was solved by
F.Bisiak,
D.E.Brodersen,
A.Chrenkova,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum
(pdb code 7qoc). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum, PDB code: 7qoc: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 7qocGo back to Magnesium Binding Sites List in 7qoc
Magnesium binding site 1 out
of 2 in the Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 7qocGo back to Magnesium Binding Sites List in 7qoc
Magnesium binding site 2 out
of 2 in the Se-Met Derivative Structure of A Small Alarmone Hydrolase (Relh) From Corynebacterium Glutamicum
Mono view Stereo pair view
Reference:
F.Bisiak,
A.Chrenkova,
S.D.Zhang,
J.N.Pedersen,
D.E.Otzen,
Y.E.Zhang,
D.E.Brodersen.
Structural Variations Between Small Alarmone Hydrolase Dimers Support Different Modes of Regulation of the Stringent Response. J.Biol.Chem. V. 298 02142 2022.
Page generated: Thu Oct 3 05:11:25 2024
ISSN: ESSN 1083-351X PubMed: 35714769 DOI: 10.1016/J.JBC.2022.102142 |
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