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Atomistry » Chlorine » PDB 3dzc-3ec0 » 3e7b | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3dzc-3ec0 » 3e7b » |
Chlorine in PDB 3e7b: Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor TautomycinEnzymatic activity of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin
All present enzymatic activity of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin:
3.1.3.16; Protein crystallography data
The structure of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin, PDB code: 3e7b
was solved by
M.S.Kelker,
R.Page,
W.Peti,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3e7b:
The structure of Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin
(pdb code 3e7b). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin, PDB code: 3e7b: Chlorine binding site 1 out of 1 in 3e7bGo back to Chlorine Binding Sites List in 3e7b
Chlorine binding site 1 out
of 1 in the Crystal Structure of Protein Phosphatase-1 Bound to the Natural Toxin Inhibitor Tautomycin
Mono view Stereo pair view
Reference:
M.S.Kelker,
R.Page,
W.Peti.
Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold For Structure-Based Drug Design of Serine/Threonine Phosphatase Inhibitors J.Mol.Biol. V. 385 11 2009.
Page generated: Sat Dec 12 09:39:46 2020
ISSN: ISSN 0022-2836 PubMed: 18992256 DOI: 10.1016/J.JMB.2008.10.053 |
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