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Atomistry » Potassium » PDB 3f2y-3gvf » 3fa0 » |
Potassium in PDB 3fa0: Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >HisEnzymatic activity of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His
All present enzymatic activity of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His:
3.2.1.17; Protein crystallography data
The structure of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His, PDB code: 3fa0
was solved by
B.H.M.Mooers,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3fa0:
The structure of Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His
(pdb code 3fa0). 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 Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His, PDB code: 3fa0: Potassium binding site 1 out of 1 in 3fa0Go back to Potassium Binding Sites List in 3fa0
Potassium binding site 1 out
of 1 in the Evaulaution at Atomic Resolution of the Role of Strain in Destabilizing the Temperature Sensitive T4 Lysozyme Mutant ARG96-- >His
Mono view Stereo pair view
Reference:
B.H.Mooers,
D.E.Tronrud,
B.W.Matthews.
Evaluation at Atomic Resolution of the Role of Strain in Destabilizing the Temperature-Sensitive T4 Lysozyme Mutant Arg 96 --> His. Protein Sci. V. 18 863 2009.
Page generated: Mon Aug 12 08:18:51 2024
ISSN: ISSN 0961-8368 PubMed: 19384984 DOI: 10.1002/PRO.93 |
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