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Calcium in PDB 5o0s: Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711Enzymatic activity of Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711
All present enzymatic activity of Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711:
3.2.1.45; Protein crystallography data
The structure of Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711, PDB code: 5o0s
was solved by
L.Wu,
W.A.Offen,
I.Z.Breen,
G.J.Davies,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711
(pdb code 5o0s). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711, PDB code: 5o0s: Calcium binding site 1 out of 1 in 5o0sGo back to Calcium Binding Sites List in 5o0s
Calcium binding site 1 out
of 1 in the Crystal Structure of TXGH116 (Beta-Glucosidase From Thermoanaerobacterium Xylolyticum) in Complex with Unreacted Beta Cyclophellitol Cyclosulfate Probe ME711
Mono view Stereo pair view
Reference:
M.Artola,
L.Wu,
M.J.Ferraz,
C.L.Kuo,
L.Raich,
I.Z.Breen,
W.A.Offen,
J.D.C.Codee,
G.A.Van Der Marel,
C.Rovira,
J.M.F.G.Aerts,
G.J.Davies,
H.S.Overkleeft.
1,6-Cyclophellitol Cyclosulfates: A New Class of Irreversible Glycosidase Inhibitor. Acs Cent Sci V. 3 784 2017.
Page generated: Sat Dec 12 05:40:49 2020
ISSN: ESSN 2374-7943 PubMed: 28776021 DOI: 10.1021/ACSCENTSCI.7B00214 |
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