Chlorine in PDB 2y5s: Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate.

All present enzymatic activity of Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate.:
2.5.1.15;

The structure of Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate., PDB code: 2y5s was solved by R.E.Morgan, G.O.Batot, J.M.Dement, V.A.Rao, T.C.Eadsforth, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.11 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.662, 86.920, 88.795, 90.00, 90.00, 90.00
R / Rfree (%)	17.564 / 21.114

The binding sites of Chlorine atom in the Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate. (pdb code 2y5s). 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 Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate., PDB code: 2y5s:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate.


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 Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1294 b:33.4 occ:1.00 OD1 A:ASP202 2.2 20.6 0.5 CG A:ASP202 2.8 23.7 0.5 N A:ASP202 3.1 21.6 1.0 N A:VAL201 3.2 20.4 1.0 OD2 A:ASP202 3.3 24.9 0.5 O A:HOH2102 3.3 20.3 1.0 CB A:VAL201 3.6 20.2 1.0 CA A:VAL201 3.7 19.5 1.0 C A:VAL201 3.8 20.6 1.0 CB A:ASP202 3.9 23.5 0.5 CB A:ASP202 3.9 24.4 0.5 N A:VAL200 3.9 21.5 1.0 CB A:ALA199 3.9 22.9 1.0 CA A:ASP202 4.0 22.4 0.5 CA A:ASP202 4.1 22.8 0.5 CG1 A:VAL200 4.1 21.0 1.0 C A:ALA199 4.1 21.1 1.0 O A:HOH2103 4.1 11.3 1.0 C A:VAL200 4.3 19.9 1.0 CG2 A:VAL201 4.5 19.1 1.0 O A:ALA199 4.5 19.7 1.0 CA A:VAL200 4.5 20.1 1.0 CA A:ALA199 4.6 22.2 1.0 CG1 A:VAL201 4.6 17.7 1.0 CB A:VAL200 5.0 20.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate.


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 Burkholderia Cenocepacia Dihydropteroate Synthase Complexed with 7,8-Dihydropteroate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1294 b:34.4 occ:1.00 N B:ASP202 3.2 22.6 1.0 N B:VAL201 3.2 21.0 1.0 CB B:VAL201 3.5 22.0 1.0 CA B:VAL201 3.7 20.8 1.0 C B:VAL201 3.9 21.2 1.0 CG B:ASP202 3.9 27.2 1.0 OD2 B:ASP202 4.0 30.7 1.0 CG1 B:VAL200 4.0 22.4 1.0 CB B:ASP202 4.0 24.9 1.0 N B:VAL200 4.0 21.1 1.0 CB B:ALA199 4.0 22.7 1.0 C B:ALA199 4.2 21.1 1.0 CA B:ASP202 4.2 23.3 1.0 OD1 B:ASP202 4.3 28.6 1.0 C B:VAL200 4.4 19.9 1.0 CG2 B:VAL201 4.5 21.1 1.0 CG1 B:VAL201 4.5 22.2 1.0 O B:ALA199 4.6 19.1 1.0 CA B:ALA199 4.6 22.4 1.0 CA B:VAL200 4.6 20.4 1.0 CB B:VAL200 5.0 21.8 1.0

R.E.Morgan, G.O.Batot, J.M.Dement, V.A.Rao, T.C.Eadsforth, W.N.Hunter. Crystal Structures of Burkholderia Cenocepacia Dihydropteroate Synthase in the Apo-Form and Complexed with the Product 7,8-Dihydropteroate. Bmc Struct.Biol. V. 11 21 2011.
ISSN: ISSN 1472-6807
PubMed: 21554707
DOI: 10.1186/1472-6807-11-21