Chlorine in PDB 5o9x: Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE

All present enzymatic activity of Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE:
5.4.2.3;

The structure of Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE, PDB code: 5o9x was solved by O.G.Raimi, R.Hurtado-Guerrero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.860, 87.574, 91.867, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.1

The binding sites of Chlorine atom in the Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE (pdb code 5o9x). 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 Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE, PDB code: 5o9x:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE


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 Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:26.8 occ:1.00 CG2 A:THR134 3.7 17.1 1.0 CG A:PRO223 3.8 19.3 1.0 CG2 A:VAL220 4.0 16.2 1.0 CB A:PRO223 4.2 17.7 1.0 CB A:PHE161 4.2 16.8 1.0 CA A:VAL220 4.3 16.0 1.0 CG2 A:VAL247 4.3 15.9 1.0 CG1 A:VAL247 4.4 16.1 1.0 CG A:PHE161 4.4 16.9 1.0 CB A:VAL247 4.5 17.2 1.0 CB A:VAL220 4.5 16.3 1.0 CD1 A:PHE161 4.7 15.6 1.0 CD A:PRO223 4.8 15.6 1.0 O A:VAL220 4.9 17.1 1.0 CE A:LYS224 5.0 22.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE


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 Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutate S69A in Complex with GLUCOSE1,6BISPHOSPHATE within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl603 b:20.3 occ:1.00 O A:HOH1116 2.1 24.1 1.0 NH1 A:ARG514 3.3 15.2 1.0 O A:HOH1071 3.4 17.6 1.0 CG A:ARG514 3.7 12.7 1.0 O A:VAL461 3.8 13.8 1.0 C A:VAL461 3.8 15.3 1.0 CD A:ARG514 3.8 15.7 1.0 CB A:ARG514 3.9 12.6 1.0 CA A:ARG462 3.9 18.2 1.0 N A:ARG462 3.9 15.0 1.0 CB A:LEU460 3.9 14.8 1.0 CB A:ARG462 4.0 18.2 1.0 N A:VAL461 4.2 14.1 1.0 CA A:ARG514 4.2 14.1 1.0 CD2 A:LEU460 4.3 13.6 1.0 CZ A:ARG514 4.4 17.3 1.0 CG A:LEU460 4.5 16.1 1.0 C A:LEU460 4.5 15.2 1.0 CA A:VAL461 4.6 13.7 1.0 NE A:ARG514 4.6 14.7 1.0 O A:HOH1045 4.6 32.8 1.0 CG A:ARG462 4.7 20.0 1.0 CA A:LEU460 4.7 15.2 1.0 N A:VAL515 4.7 15.4 1.0 CD1 A:LEU460 4.8 15.2 1.0 O A:VAL515 4.8 15.0 1.0 O A:HOH1118 4.9 33.7 1.0 O A:HOH735 4.9 24.7 1.0 C A:ARG514 5.0 14.3 1.0

O.G.Raimi, R.Hurtado-Guerrero, D.M.F.Van Aalten. Evidence For Substrate-Assisted Catalysis Inn-Acetylphosphoglucosamine Mutase. Biochem. J. V. 475 2547 2018.
ISSN: ESSN 1470-8728
PubMed: 29967067
DOI: 10.1042/BCJ20180172