Chlorine in PDB 6m2u: The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp

The structure of The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp, PDB code: 6m2u was solved by T.L.Li, K.Adhikari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.82 / 1.71
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.524, 94.656, 94.355, 90, 104.98, 90
R / Rfree (%)	17 / 20.6

The binding sites of Chlorine atom in the The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp (pdb code 6m2u). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp, PDB code: 6m2u:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:31.5 occ:1.00 CL2 A:F0O602 0.0 31.5 1.0 C2 A:F0O602 1.8 16.7 1.0 O A:HOH1200 2.4 14.5 1.0 N1 A:F0O602 2.7 14.6 1.0 CA A:ALA333 3.1 7.8 1.0 S1 A:F0O602 3.1 34.9 1.0 O A:HOH1020 3.3 10.0 1.0 N A:ALA334 3.3 9.5 1.0 C A:ALA333 3.4 7.5 1.0 CD1 A:TYR228 3.7 7.2 1.0 O A:HOH1002 3.7 18.8 1.0 CB A:ALA333 3.7 6.6 1.0 O A:LEU332 3.9 9.3 1.0 C3 A:F0O602 3.9 13.6 1.0 CA A:TYR228 3.9 6.1 1.0 CA A:GLY327 4.1 8.0 1.0 N A:ALA333 4.2 7.6 1.0 CA A:ALA334 4.2 8.5 1.0 C4 A:F0O602 4.2 16.2 1.0 CB A:TYR228 4.3 6.4 1.0 O A:ALA333 4.3 9.1 1.0 CG A:TYR228 4.4 5.6 1.0 C A:LEU332 4.5 8.6 1.0 N A:TYR228 4.5 6.5 1.0 N A:GLY327 4.5 8.9 1.0 CB A:ALA334 4.6 10.0 1.0 CE1 A:TYR228 4.6 6.9 1.0 O A:HOH788 4.6 10.7 1.0 H3 A:F0O602 4.7 16.3 1.0 O A:ALA227 4.9 5.7 1.0 O A:HOH1115 4.9 14.0 1.0 C A:GLY327 4.9 9.2 1.0 C A:ALA227 4.9 5.8 1.0 O A:TYR228 5.0 6.4 1.0

Chlorine binding site 2 out of 2 in the The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of The Crystal Structure of Benzoate Coenzyme A Ligase Double Mutant (H333A/I334A) in Complex with 2-Chloro-1,3-Thiazole-5-Carboxylate-Amp within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl602 b:36.7 occ:1.00 CL2 B:F0O602 0.0 36.7 1.0 C2 B:F0O602 1.8 18.4 1.0 N1 B:F0O602 2.7 19.6 1.0 CA B:ALA333 3.0 7.5 1.0 S1 B:F0O602 3.1 39.5 1.0 O B:HOH955 3.2 11.2 1.0 N B:ALA334 3.3 8.8 1.0 C B:ALA333 3.4 7.6 1.0 CB B:ALA333 3.7 7.8 1.0 CD1 B:TYR228 3.8 9.9 1.0 O B:LEU332 3.8 8.3 1.0 CA B:TYR228 3.9 7.0 1.0 C3 B:F0O602 3.9 20.5 1.0 O B:HOH839 4.1 19.3 1.0 N B:ALA333 4.1 7.9 1.0 CA B:ALA334 4.2 8.1 1.0 CA B:GLY327 4.2 8.7 1.0 CB B:TYR228 4.2 6.0 1.0 O B:ALA333 4.3 7.9 1.0 C4 B:F0O602 4.3 22.0 1.0 C B:LEU332 4.4 8.8 1.0 N B:TYR228 4.4 6.2 1.0 CG B:TYR228 4.5 6.2 1.0 N B:GLY327 4.5 8.3 1.0 CB B:ALA334 4.5 9.7 1.0 O B:HOH776 4.5 9.6 1.0 CE1 B:TYR228 4.7 6.8 1.0 H3 B:F0O602 4.7 24.6 1.0 O B:ALA227 4.8 5.8 1.0 C B:ALA227 4.8 6.0 1.0 C B:TYR228 5.0 5.7 1.0 C B:GLY327 5.0 12.4 1.0 O B:TYR228 5.0 6.2 1.0

K.Adhikari, I.W.Lo, C.L.Chen, Y.L.Wang, K.H.Lin, S.M.Zadeh, R.Rattinam, Y.S.Li, C.J.Wu, T.L.Li. Chemoenzymatic Synthesis and Biological Evaluation For Bioactive Molecules Derived From Bacterial Benzoyl Coenzyme A Ligase and Plant Type III Polyketide Synthase. Biomolecules V. 10 2020.
ISSN: ESSN 2218-273X
PubMed: 32397467
DOI: 10.3390/BIOM10050738