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Atomistry » Zinc » PDB 5m2z-5mcv » 5m9w | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 5m2z-5mcv » 5m9w » |
Zinc in PDB 5m9w: Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65.Enzymatic activity of Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65.
All present enzymatic activity of Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65.:
3.4.24.27; Protein crystallography data
The structure of Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65., PDB code: 5m9w
was solved by
S.G.Krimmer,
J.Cramer,
A.Heine,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5m9w:
The structure of Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65.
(pdb code 5m9w). 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 Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65., PDB code: 5m9w: Zinc binding site 1 out of 1 in 5m9wGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Experimental Mad Phased Structure of Thermolysin in Complex with Inhibitor JC65.
![]() Mono view ![]() Stereo pair view
Reference:
S.G.Krimmer,
J.Cramer,
J.Schiebel,
A.Heine,
G.Klebe.
How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1' Pocket of Thermolysin. J. Am. Chem. Soc. V. 139 10419 2017.
Page generated: Sun Oct 27 22:02:19 2024
ISSN: ESSN 1520-5126 PubMed: 28696673 DOI: 10.1021/JACS.7B05028 |
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