Chlorine in PDB 2vb9: Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure

All present enzymatic activity of Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure:
2.3.1.41;

The structure of Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure, PDB code: 2vb9 was solved by G.Pappenberger, T.Schulz-Gasch, J.Bailly, M.Hennig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	115.47 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.914, 138.355, 211.914, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 23.8

The binding sites of Chlorine atom in the Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure (pdb code 2vb9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure, PDB code: 2vb9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1405 b:68.7 occ:1.00 O A:HOH2497 3.0 46.9 1.0 NH2 A:ARG27 3.1 30.5 1.0 ND1 A:HIS352 3.4 24.4 1.0 NH1 A:ARG27 3.9 31.1 1.0 O A:HOH2500 3.9 45.6 1.0 CZ A:ARG27 4.0 29.0 1.0 CE1 A:HIS352 4.2 26.3 1.0 CG A:HIS352 4.4 25.2 1.0 CB A:HIS352 4.6 23.4 1.0 CD2 A:LEU23 5.0 22.5 1.0

Chlorine binding site 2 out of 2 in the Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Beta-Ketoacyl-Acp Synthase I (Kas) From E. Coli, Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1405 b:40.9 occ:1.00 O B:HOH2096 2.8 55.3 1.0 ND1 B:HIS352 3.2 14.2 1.0 O B:HOH2531 3.6 37.7 1.0 NH2 B:ARG27 3.6 20.7 1.0 NH1 B:ARG27 3.8 20.6 1.0 CE1 B:HIS352 3.9 15.3 1.0 CZ B:ARG27 4.2 19.7 1.0 CG B:HIS352 4.3 13.2 1.0 CB B:HIS352 4.6 13.1 1.0 O B:HOH2529 4.7 42.6 1.0 O B:HOH2095 4.7 31.1 1.0 O B:HOH2014 4.9 49.6 1.0

G.Pappenberger, T.Schulz-Gasch, E.Kusznir, F.Mueller, M.Hennig. Structure-Assisted Discovery of An Aminothiazole Derivative As A Lead Molecule For Inhibition of Bacterial Fatty-Acid Synthesis. Acta Crystallogr.,Sect.D V. 63 1208 2007.
ISSN: ISSN 0907-4449
PubMed: 18084068
DOI: 10.1107/S0907444907049852