Chlorine in PDB 7bly: Structure of the Chitin Deacetylase Angcda From Aspergillus Niger
Enzymatic activity of Structure of the Chitin Deacetylase Angcda From Aspergillus Niger
All present enzymatic activity of Structure of the Chitin Deacetylase Angcda From Aspergillus Niger:
3.5.1.41;
3.5.1.41;
Protein crystallography data
The structure of Structure of the Chitin Deacetylase Angcda From Aspergillus Niger, PDB code: 7bly
was solved by
T.Roret,
M.Bonin,
L.Hembach,
B.M.Moerschbacher,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 42.38 / 1.81 |
| Space group | P 4 3 2 |
| Cell size a, b, c (Å), α, β, γ (°) | 119.874, 119.874, 119.874, 90, 90, 90 |
| R / Rfree (%) | 15.3 / 18.6 |
Other elements in 7bly:
The structure of Structure of the Chitin Deacetylase Angcda From Aspergillus Niger also contains other interesting chemical elements:
| Zinc | (Zn) | 1 atom |
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of the Chitin Deacetylase Angcda From Aspergillus Niger
(pdb code 7bly). 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 Structure of the Chitin Deacetylase Angcda From Aspergillus Niger, PDB code: 7bly:
In total only one binding site of Chlorine was determined in the Structure of the Chitin Deacetylase Angcda From Aspergillus Niger, PDB code: 7bly:
Chlorine binding site 1 out of 1 in 7bly
Go back to
Chlorine Binding Sites List in 7bly
Chlorine binding site 1 out
of 1 in the Structure of the Chitin Deacetylase Angcda From Aspergillus Niger
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Chlorine with other atoms in the Cl binding
site number 1 of Structure of the Chitin Deacetylase Angcda From Aspergillus Niger within 5.0Å range:
|
Reference:
M.Bonin,
L.Hameleers,
L.Hembach,
T.Roret,
S.Cord-Landwehr,
G.Michel,
B.M.Moerschbacher.
In Depths Analysis of An Aspergillus Niger Chitin Deacetylase Using in Silico and in Vitro Methods to Decipher Its Subsite Preferences To Be Published.
Page generated: Fri Sep 24 12:50:44 2021
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