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Atomistry » Zinc » PDB 5t75-5thi » 5tae » |
Zinc in PDB 5tae: Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme ThermolysinEnzymatic activity of Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin
All present enzymatic activity of Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin:
3.4.24.27; Protein crystallography data
The structure of Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin, PDB code: 5tae
was solved by
M.Dong,
B.J.Bahnson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5tae:
The structure of Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin
(pdb code 5tae). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin, PDB code: 5tae: Zinc binding site 1 out of 1 in 5taeGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin
![]() Mono view ![]() Stereo pair view
Reference:
M.Dong,
B.J.Bahnson.
Conformational Sampling Differences Across the Arrhenius Plot Biphasic Break Point at Ambient Temperature in the Enzyme Thermolysin To Be Published.
Page generated: Thu Aug 21 08:52:31 2025
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