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Calcium in PDB 5z5h: Crystal Structure of A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-XyloseEnzymatic activity of Crystal Structure of A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose
All present enzymatic activity of Crystal Structure of A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose:
3.2.1.37; Protein crystallography data
The structure of Crystal Structure of A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose, PDB code: 5z5h
was solved by
A.Rohman,
N.Van Oosterwijk,
N.N.T.Puspaningsih,
B.W.Dijkstra,
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 A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose
(pdb code 5z5h). 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 A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose, PDB code: 5z5h: Calcium binding site 1 out of 1 in 5z5hGo back to Calcium Binding Sites List in 5z5h
Calcium binding site 1 out
of 1 in the Crystal Structure of A Thermostable Glycoside Hydrolase Family 43 {Beta}-1,4-Xylosidase From Geobacillus Thermoleovorans It-08 in Complex with D-Xylose
Mono view Stereo pair view
Reference:
A.Rohman,
N.Van Oosterwijk,
N.N.T.Puspaningsih,
B.W.Dijkstra.
Structural Basis of Product Inhibition By Arabinose and Xylose of the Thermostable GH43 Beta-1,4-Xylosidase From Geobacillus Thermoleovorans It-08. Plos One V. 13 96358 2018.
Page generated: Sat Dec 12 05:55:31 2020
ISSN: ESSN 1932-6203 PubMed: 29698436 DOI: 10.1371/JOURNAL.PONE.0196358 |
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