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Atomistry » Magnesium » PDB 6rux-6s40 » 6s36 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 6rux-6s40 » 6s36 » |
Magnesium in PDB 6s36: Crystal Structure of E. Coli Adenylate Kinase R119K MutantEnzymatic activity of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant
All present enzymatic activity of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant:
2.7.4.3; Protein crystallography data
The structure of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant, PDB code: 6s36
was solved by
C.Grundstrom,
P.Rogne,
M.Wolf-Watz,
A.E.Sauer-Eriksson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6s36:
The structure of Crystal Structure of E. Coli Adenylate Kinase R119K Mutant also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant
(pdb code 6s36). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant, PDB code: 6s36: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 6s36Go back to Magnesium Binding Sites List in 6s36
Magnesium binding site 1 out
of 2 in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 6s36Go back to Magnesium Binding Sites List in 6s36
Magnesium binding site 2 out
of 2 in the Crystal Structure of E. Coli Adenylate Kinase R119K Mutant
Mono view Stereo pair view
Reference:
P.Rogne,
D.Andersson,
C.Grundstrom,
E.Sauer-Eriksson,
A.Linusson,
M.Wolf-Watz.
Nucleation of An Activating Conformational Change By A Cation-Pi Interaction. Biochemistry V. 58 3408 2019.
Page generated: Tue Oct 1 17:37:14 2024
ISSN: ISSN 0006-2960 PubMed: 31339702 DOI: 10.1021/ACS.BIOCHEM.9B00538 |
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