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| Atomistry » Chlorine » PDB 5ead-5ehw » 5eff | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Atomistry » Chlorine » PDB 5ead-5ehw » 5eff » |
Chlorine in PDB 5eff: Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27Enzymatic activity of Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27
All present enzymatic activity of Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27:
3.2.1.8; Protein crystallography data
The structure of Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27, PDB code: 5eff
was solved by
P.Mahanta,
A.Bhardwaj,
V.S.Reddy,
S.Ramakumar,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5eff:
The structure of Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27 also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27
(pdb code 5eff). 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 An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27, PDB code: 5eff: Chlorine binding site 1 out of 1 in 5effGo back to
Chlorine binding site 1 out
of 1 in the Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27
![]() Mono view ![]() Stereo pair view
Reference:
P.Mahanta,
A.Bhardwaj,
V.S.Reddy,
S.Ramakumar.
Crystal Structure of An Aromatic Mutant (F4A) of An Alkali Thermostable GH10 Xylanase From Bacillus Sp. Ng-27 To Be Published.
Page generated: Sat Jul 12 01:41:16 2025
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