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Atomistry » Magnesium » PDB 6qux-6r5i » 6r5i | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6qux-6r5i » 6r5i » |
Magnesium in PDB 6r5i: The Crystal Structure of the Glycoside Hydrolase Bglx From P. AeruginosaProtein crystallography data
The structure of The Crystal Structure of the Glycoside Hydrolase Bglx From P. Aeruginosa, PDB code: 6r5i
was solved by
M.T.Batuecas,
J.A.Hermoso,
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 The Crystal Structure of the Glycoside Hydrolase Bglx From P. Aeruginosa
(pdb code 6r5i). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of the Glycoside Hydrolase Bglx From P. Aeruginosa, PDB code: 6r5i: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6r5iGo back to Magnesium Binding Sites List in 6r5i
Magnesium binding site 1 out
of 2 in the The Crystal Structure of the Glycoside Hydrolase Bglx From P. Aeruginosa
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6r5iGo back to Magnesium Binding Sites List in 6r5i
Magnesium binding site 2 out
of 2 in the The Crystal Structure of the Glycoside Hydrolase Bglx From P. Aeruginosa
Mono view Stereo pair view
Reference:
K.V.Mahasenan,
M.T.Batuecas,
S.De Benedetti,
C.Kim,
N.Rana,
M.Lee,
D.Hesek,
J.F.Fisher,
J.Sanz-Aparicio,
J.A.Hermoso,
S.Mobashery.
Catalytic Cycle of Glycoside Hydrolase Bglx Frompseudomonas Aeruginosaand Its Implications For Biofilm Formation. Acs Chem.Biol. V. 15 189 2020.
Page generated: Tue Oct 1 16:34:31 2024
ISSN: ESSN 1554-8937 PubMed: 31877028 DOI: 10.1021/ACSCHEMBIO.9B00754 |
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