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Chlorine in PDB 6qbu: Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188Enzymatic activity of Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188
All present enzymatic activity of Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188:
3.4.21.36; Protein crystallography data
The structure of Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188, PDB code: 6qbu
was solved by
J.A.Brito,
V.T.Almeida,
L.M.Carvalho,
R.Moreira,
M.Archer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6qbu:
The structure of Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188
(pdb code 6qbu). 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 Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188, PDB code: 6qbu: Chlorine binding site 1 out of 1 in 6qbuGo back to Chlorine Binding Sites List in 6qbu
Chlorine binding site 1 out
of 1 in the Crystal Structure of Porcine Pancreatic Elastase (Ppe) in Complex with the 3-Oxo-Beta-Sultam Inhibitor LMC188
Mono view Stereo pair view
Reference:
L.A.R.Carvalho,
V.T.Almeida,
J.A.Brito,
K.M.Lum,
T.F.Oliveira,
R.C.Guedes,
L.M.Goncalves,
S.D.Lucas,
B.F.Cravatt,
M.Archer,
R.Moreira.
3-Oxo-Beta-Sultam As A Sulfonylating Chemotype For Inhibition of Serine Hydrolases and Activity-Based Protein Profiling. Acs Chem.Biol. 2020.
Page generated: Sat Dec 12 13:33:20 2020
ISSN: ESSN 1554-8937 PubMed: 32176480 DOI: 10.1021/ACSCHEMBIO.0C00090 |
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