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Atomistry » Potassium » PDB 4eei-4gx0 » 4g38 » |
Potassium in PDB 4g38: Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton TransferEnzymatic activity of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
All present enzymatic activity of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer:
1.8.1.2; Protein crystallography data
The structure of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer, PDB code: 4g38
was solved by
K.W.Smith,
M.E.Stroupe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4g38:
The structure of Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
(pdb code 4g38). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer, PDB code: 4g38: Potassium binding site 1 out of 1 in 4g38Go back to Potassium Binding Sites List in 4g38
Potassium binding site 1 out
of 1 in the Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer
Mono view Stereo pair view
Reference:
K.W.Smith,
M.E.Stroupe.
Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism For Coordinated Electron and Proton Transfer. Biochemistry V. 51 9857 2012.
Page generated: Mon Aug 12 10:47:37 2024
ISSN: ISSN 0006-2960 PubMed: 23153334 DOI: 10.1021/BI300947A |
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