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Atomistry » Chlorine » PDB 3vfc-3vm5 » 3vik | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3vfc-3vm5 » 3vik » |
Chlorine in PDB 3vik: Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with CellobioseEnzymatic activity of Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose
All present enzymatic activity of Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose:
3.2.1.21; Protein crystallography data
The structure of Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose, PDB code: 3vik
was solved by
W.Y.Jeng,
C.I.Liu,
A.H.J.Wang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3vik:
The structure of Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose
(pdb code 3vik). 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 Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose, PDB code: 3vik: Chlorine binding site 1 out of 1 in 3vikGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Beta-Glucosidase From Termite Neotermes Koshunensis in Complex with Cellobiose
![]() Mono view ![]() Stereo pair view
Reference:
W.Y.Jeng,
N.C.Wang,
C.T.Lin,
W.J.Chang,
C.I.Liu,
A.H.J.Wang.
High-Resolution Structures of Neotermes Koshunensis Beta-Glucosidase Mutants Provide Insights Into the Catalytic Mechanism and the Synthesis of Glucoconjugates Acta Crystallogr.,Sect.D V. 68 829 2012.
Page generated: Fri Jul 11 11:42:33 2025
ISSN: ISSN 0907-4449 PubMed: 22751668 DOI: 10.1107/S0907444912013224 |
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