Chlorine in PDB 3ay7: Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant

All present enzymatic activity of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant:
1.1.1.47;

The structure of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant, PDB code: 3ay7 was solved by T.Nishioka, Y.Yasutake, Y.Nishiya, T.Tamura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.45 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.116, 128.260, 64.641, 90.00, 110.73, 90.00
R / Rfree (%)	20 / 24.6

The binding sites of Chlorine atom in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant (pdb code 3ay7). 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 Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant, PDB code: 3ay7:

Chlorine binding site 1 out of 1 in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 G259A Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl262 b:28.8 occ:1.00 OG B:SER255 3.0 28.6 1.0 N B:SER255 3.4 27.7 1.0 CB B:SER255 3.6 28.7 1.0 CD B:PRO254 3.7 24.6 1.0 N B:PRO254 3.7 25.0 1.0 CA B:TYR253 3.8 22.2 1.0 C B:TYR253 3.8 23.4 1.0 CB B:TYR253 3.9 21.2 1.0 CD2 B:TYR253 4.1 17.8 1.0 CA B:SER255 4.1 28.2 1.0 CG B:PRO254 4.3 26.8 1.0 CG B:TYR253 4.4 20.6 1.0 C B:PRO254 4.4 27.1 1.0 O B:TYR253 4.5 24.0 1.0 CA B:PRO254 4.6 26.2 1.0 CB B:PRO254 4.9 27.2 1.0 CD1 B:PHE256 5.0 26.0 1.0

T.Nishioka, Y.Yasutake, Y.Nishiya, T.Tamura. Structure-Guided Mutagenesis For the Improvement of Substrate SpecifiCity of Bacillus Megaterium Glucose 1-Dehydrogenase IV Febs J. V. 279 3264 2012.
ISSN: ISSN 1742-464X
PubMed: 22804868
DOI: 10.1111/J.1742-4658.2012.08713.X