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Chlorine in PDB 6r1o: Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine DerivativeEnzymatic activity of Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative
All present enzymatic activity of Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative:
6.1.1.11; Protein crystallography data
The structure of Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative, PDB code: 6r1o
was solved by
R.Salimraj,
R.Cain,
D.I.Roper,
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 E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative
(pdb code 6r1o). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative, PDB code: 6r1o: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 6r1oGo back to Chlorine Binding Sites List in 6r1o
Chlorine binding site 1 out
of 2 in the Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 6r1oGo back to Chlorine Binding Sites List in 6r1o
Chlorine binding site 2 out
of 2 in the Crystal Structure of E. Coli Seryl-Trna Synthetase Complexed to A Seryl Sulfamoyl Adenosine Derivative
Mono view Stereo pair view
Reference:
R.Cain,
R.Salimraj,
A.S.Punekar,
D.Bellini,
C.W.G.Fishwick,
L.Czaplewski,
D.J.Scott,
G.Harris,
C.G.Dowson,
A.J.Lloyd,
D.I.Roper.
Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-Trna Synthetase. J.Med.Chem. V. 62 9703 2019.
Page generated: Sat Dec 12 13:35:22 2020
ISSN: ISSN 0022-2623 PubMed: 31626547 DOI: 10.1021/ACS.JMEDCHEM.9B01131 |
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