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Atomistry » Sodium » PDB 6xyt-6ycq » 6y6y | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 6xyt-6ycq » 6y6y » |
Sodium in PDB 6y6y: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129AEnzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A
All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A:
1.7.2.4; Protein crystallography data
The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A, PDB code: 6y6y
was solved by
L.Zhang,
P.M.H.Kroneck,
O.Einsle,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6y6y:
The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A
(pdb code 6y6y). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A, PDB code: 6y6y: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 6y6yGo back to Sodium Binding Sites List in 6y6y
Sodium binding site 1 out
of 2 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 6y6yGo back to Sodium Binding Sites List in 6y6y
Sodium binding site 2 out
of 2 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H129A
Mono view Stereo pair view
Reference:
L.Zhang,
E.Bill,
P.M.H.Kroneck,
O.Einsle.
A [3CU:2S] Cluster Provides Insight Into the Assembly and Function of the Cuz Site of Nitrous Oxide Reductase Chem Sci 2021.
Page generated: Tue Oct 8 14:57:50 2024
ISSN: ESSN 2041-6539 DOI: 10.1039/D0SC05204C |
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