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Atomistry » Magnesium » PDB 6q70-6qiu » 6q70 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6q70-6qiu » 6q70 » |
Magnesium in PDB 6q70: Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of HepesEnzymatic activity of Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes
All present enzymatic activity of Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes:
5.1.1.1; Protein crystallography data
The structure of Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes, PDB code: 6q70
was solved by
N.Bernardo-Garcia,
F.Gago,
J.A.Hermoso,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6q70:
The structure of Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes
(pdb code 6q70). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes, PDB code: 6q70: Magnesium binding site 1 out of 1 in 6q70Go back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystal Structure of the Alanine Racemase BSU17640 From Bacillus Subtilis in the Presence of Hepes
![]() Mono view ![]() Stereo pair view
Reference:
N.Bernardo-Garcia,
P.A.Sanchez-Murcia,
A.Espaillat,
S.Martinez-Caballero,
F.Cava,
J.A.Hermoso,
F.Gago.
Cold-Induced Aldimine Bond Cleavage By Tris in Bacillus Subtilis Alanine Racemase. Org.Biomol.Chem. V. 17 4350 2019.
Page generated: Tue Oct 1 15:25:19 2024
ISSN: ESSN 1477-0539 PubMed: 30977502 DOI: 10.1039/C9OB00223E |
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