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Atomistry » Chlorine » PDB 5fjj-5frd » 5fom » |
Chlorine in PDB 5fom: Crystal Structure of the Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426Enzymatic activity of Crystal Structure of the Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426
All present enzymatic activity of Crystal Structure of the Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426:
6.1.1.4; Protein crystallography data
The structure of Crystal Structure of the Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426, PDB code: 5fom
was solved by
A.Palencia,
R.J.Liu,
M.Lukarska,
J.Gut,
A.Bougdour,
B.Touquet,
E.D.Wang,
M.R.K.Alley,
P.J.Rosenthal,
M.A.Hakimi,
S.Cusack,
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 Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426
(pdb code 5fom). 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 Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426, PDB code: 5fom: Chlorine binding site 1 out of 1 in 5fomGo back to Chlorine Binding Sites List in 5fom
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Cryptosporidium Muris Cytosolic Leucyl-Trna Synthetase Editing Domain Complex with the Adduct Amp-AN6426
Mono view Stereo pair view
Reference:
A.Palencia,
R.Liu,
M.Lukarska,
J.Gut,
A.Bougdour,
B.Touquet,
E.Wang,
X.Li,
M.R.K.Alley,
Y.R.Freund,
P.J.Rosenthal,
M.Hakimi,
S.Cusack.
Cryptosporidium and Toxoplasma Parasites Are Inhibited By A Benzoxaborole Targeting Leucyl-Trna Synthetase. Antimicrob.Agents Chemother. V. 60 5817 2016.
Page generated: Fri Jul 26 08:06:23 2024
ISSN: ISSN 0066-4804 PubMed: 27431220 DOI: 10.1128/AAC.00873-16 |
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