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Chlorine in PDB 5ncx: Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent InhibitorEnzymatic activity of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor
All present enzymatic activity of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor:
3.2.1.45; Protein crystallography data
The structure of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor, PDB code: 5ncx
was solved by
G.J.Davies,
I.Z.Breen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ncx:
The structure of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor
(pdb code 5ncx). 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 Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor, PDB code: 5ncx: Chlorine binding site 1 out of 1 in 5ncxGo back to Chlorine Binding Sites List in 5ncx
Chlorine binding site 1 out
of 1 in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor
Mono view Stereo pair view
Reference:
D.Lahav,
B.Liu,
R.J.B.H.N.Van Den Berg,
A.M.C.H.Van Den Nieuwendijk,
T.Wennekes,
A.T.Ghisaidoobe,
I.Breen,
M.J.Ferraz,
C.L.Kuo,
L.Wu,
P.P.Geurink,
H.Ovaa,
G.A.Van Der Marel,
M.Van Der Stelt,
R.G.Boot,
G.J.Davies,
J.M.F.G.Aerts,
H.S.Overkleeft.
A Fluorescence Polarization Activity-Based Protein Profiling Assay in the Discovery of Potent, Selective Inhibitors For Human Nonlysosomal Glucosylceramidase. J. Am. Chem. Soc. V. 139 14192 2017.
Page generated: Sat Dec 12 12:09:16 2020
ISSN: ESSN 1520-5126 PubMed: 28937220 DOI: 10.1021/JACS.7B07352 |
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