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Atomistry » Chlorine » PDB 5nz7-5o5t » 5o5m | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5nz7-5o5t » 5o5m » |
Chlorine in PDB 5o5m: Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117Enzymatic activity of Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117
All present enzymatic activity of Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117:
2.7.11.11; Protein crystallography data
The structure of Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117, PDB code: 5o5m
was solved by
J.M.Mueller,
A.Heine,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117
(pdb code 5o5m). 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 the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117, PDB code: 5o5m: Chlorine binding site 1 out of 1 in 5o5mGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Protein-Kinase A Catalytic Subunit From Criteculus Griseus in Complex with Compounds RKP120 and RKP117
![]() Mono view ![]() Stereo pair view
Reference:
J.M.Mueller,
R.Kirschner,
A.Geyer,
G.Klebe.
Conceptional Design of Self-Assembling Bisubstrate-Like Inhibitors of Protein Kinase A Resulting in A Boronic Acid Glutamate Linkage Acs Omega 2019.
Page generated: Sat Jul 12 06:33:05 2025
ISSN: ESSN 2470-1343 DOI: 10.1021/ACSOMEGA.8B02364 |
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