Chlorine in PDB 3ay6: Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose

All present enzymatic activity of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose:
1.1.1.47;

The structure of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose, PDB code: 3ay6 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)	28.68 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.143, 127.033, 88.661, 90.00, 94.94, 90.00
R / Rfree (%)	19.4 / 23.5

The binding sites of Chlorine atom in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose (pdb code 3ay6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose, PDB code: 3ay6:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose


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 A258F Mutant in Complex with Nadh and D-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl264 b:22.2 occ:1.00 OG C:SER255 3.0 26.6 1.0 OG A:SER255 3.1 26.5 1.0 N C:SER255 3.5 23.0 1.0 N A:SER255 3.5 25.1 1.0 CB C:SER255 3.7 24.4 1.0 CD C:PRO254 3.7 21.7 1.0 N A:PRO254 3.7 22.4 1.0 N C:PRO254 3.7 21.9 1.0 CB A:SER255 3.7 26.2 1.0 C A:TYR253 3.8 21.8 1.0 CD A:PRO254 3.8 22.5 1.0 CA A:TYR253 3.8 20.5 1.0 C C:TYR253 3.8 21.1 1.0 CA C:TYR253 3.8 20.3 1.0 CB A:TYR253 4.1 19.8 1.0 CG C:PRO254 4.1 23.2 1.0 CG A:PRO254 4.1 23.7 1.0 CB C:TYR253 4.1 19.7 1.0 CA C:SER255 4.2 23.9 1.0 CA A:SER255 4.2 25.8 1.0 CD2 A:TYR253 4.3 16.3 1.0 CD2 C:TYR253 4.3 17.0 1.0 O A:TYR253 4.4 22.1 1.0 O C:TYR253 4.5 21.2 1.0 C C:PRO254 4.5 22.5 1.0 C A:PRO254 4.5 24.3 1.0 CA C:PRO254 4.6 22.1 1.0 CA A:PRO254 4.6 23.9 1.0 CG A:TYR253 4.6 18.1 1.0 CG C:TYR253 4.7 19.1 1.0 CD1 C:PHE256 4.9 16.6 1.0 CD1 A:PHE256 4.9 26.1 1.0 CB C:PRO254 4.9 22.0 1.0 CB A:PRO254 5.0 23.8 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Bacillus Megaterium Glucose Dehydrogenase 4 A258F Mutant in Complex with Nadh and D-Glucose within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl264 b:23.3 occ:1.00 OG D:SER255 3.2 25.4 1.0 OG B:SER255 3.2 30.0 1.0 N B:SER255 3.5 27.4 1.0 N D:SER255 3.6 23.2 1.0 CB B:SER255 3.6 28.3 1.0 CD B:PRO254 3.7 24.3 1.0 N D:PRO254 3.7 21.6 1.0 N B:PRO254 3.7 24.0 1.0 CD D:PRO254 3.7 21.7 1.0 C D:TYR253 3.8 21.3 1.0 CA D:TYR253 3.8 20.4 1.0 C B:TYR253 3.8 23.2 1.0 CA B:TYR253 3.8 22.1 1.0 CB D:SER255 3.9 24.9 1.0 CB B:TYR253 4.1 21.8 1.0 CG D:PRO254 4.1 23.0 1.0 CA B:SER255 4.2 28.4 1.0 CB D:TYR253 4.2 20.2 1.0 CG B:PRO254 4.2 25.2 1.0 CD2 B:TYR253 4.2 21.5 1.0 CA D:SER255 4.3 24.2 1.0 CD2 D:TYR253 4.3 18.5 1.0 O D:TYR253 4.4 21.1 1.0 O B:TYR253 4.5 22.4 1.0 C D:PRO254 4.5 22.9 1.0 CA D:PRO254 4.5 22.6 1.0 C B:PRO254 4.5 26.4 1.0 CG B:TYR253 4.6 21.2 1.0 CA B:PRO254 4.6 25.4 1.0 CG D:TYR253 4.7 19.9 1.0 CD1 B:PHE256 4.8 27.1 1.0 CB D:PRO254 4.8 22.9 1.0 CE1 B:PHE256 4.9 27.4 1.0 CD1 D:PHE256 5.0 18.7 1.0 CB B:PRO254 5.0 24.7 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