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Atomistry » Sodium » PDB 7pfi-7q77 » 7pfr » |
Sodium in PDB 7pfr: Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces GriseoflavusEnzymatic activity of Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus
All present enzymatic activity of Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus:
1.10.3.2; Protein crystallography data
The structure of Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus, PDB code: 7pfr
was solved by
A.Gabdulkhakov,
S.Tishchenko,
I.Kolyadenko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7pfr:
The structure of Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus
(pdb code 7pfr). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus, PDB code: 7pfr: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 7pfrGo back to Sodium Binding Sites List in 7pfr
Sodium binding site 1 out
of 2 in the Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 7pfrGo back to Sodium Binding Sites List in 7pfr
Sodium binding site 2 out
of 2 in the Crystal Structure of Two-Domain Laccase Mutant M199A From Streptomyces Griseoflavus
Mono view Stereo pair view
Reference:
I.Kolyadenko,
A.Scherbakova,
K.Kovalev,
A.Gabdulkhakov,
S.Tishchenko.
Engineering the Catalytic Properties of Two-Domain Laccase From Streptomyces Griseoflavus Ac-993. Int J Mol Sci V. 23 2021.
Page generated: Tue Oct 8 18:31:44 2024
ISSN: ESSN 1422-0067 PubMed: 35008493 DOI: 10.3390/IJMS23010065 |
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