Chlorine in PDB 4b3u: Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor

All present enzymatic activity of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor:
2.7.7.24;

The structure of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor, PDB code: 4b3u was solved by M.S.Alphey, L.Pirrie, L.S.Torrie, M.Gardiner, A.Sarkar, R.Brenk, N.J.Westwood, D.Gray, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.13 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	64.210, 154.580, 134.030, 90.00, 92.05, 90.00
R / Rfree (%)	21.8 / 26.2

The binding sites of Chlorine atom in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor (pdb code 4b3u). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor, PDB code: 4b3u:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1294 b:39.5 occ:1.00 ND1 A:HIS116 2.9 40.8 1.0 CA A:HIS116 3.8 38.1 1.0 CG A:HIS116 3.8 38.4 1.0 CE1 A:HIS116 3.8 41.8 1.0 N A:ASP117 3.9 46.1 1.0 O A:HOH2235 3.9 41.0 1.0 CB A:HIS116 4.0 39.1 1.0 C A:HIS116 4.4 42.6 1.0 O A:GLY115 4.7 34.0 1.0 OD1 A:ASP117 4.8 62.4 1.0 CAR A:NWL400 4.9 44.9 1.0 N A:HIS116 4.9 31.4 1.0 CA A:ASP117 5.0 51.1 1.0 NE2 A:HIS116 5.0 43.8 1.0

Chlorine binding site 2 out of 4 in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1294 b:41.4 occ:1.00 ND1 B:HIS116 3.0 43.0 1.0 CA B:HIS116 3.7 37.5 1.0 N B:ASP117 3.8 43.6 1.0 O B:HOH2212 3.8 43.7 1.0 CG B:HIS116 3.9 40.6 1.0 CE1 B:HIS116 4.0 39.7 1.0 CB B:HIS116 4.0 38.9 1.0 C B:HIS116 4.3 40.3 1.0 O B:GLY115 4.5 34.0 1.0 N B:HIS116 4.8 34.4 1.0 CA B:ASP117 4.9 49.6 1.0

Chlorine binding site 3 out of 4 in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1294 b:41.0 occ:1.00 ND1 C:HIS116 2.7 43.6 1.0 O C:HOH2085 3.2 43.2 1.0 CE1 C:HIS116 3.6 41.8 1.0 CG C:HIS116 3.7 39.6 1.0 CA C:HIS116 3.8 37.5 1.0 N C:ASP117 3.9 44.4 1.0 CB C:HIS116 4.0 38.3 1.0 C C:HIS116 4.4 41.2 1.0 O C:GLY115 4.7 31.0 1.0 NE2 C:HIS116 4.8 40.3 1.0 CD2 C:HIS116 4.8 40.5 1.0 N C:HIS116 4.9 32.3 1.0

Chlorine binding site 4 out of 4 in the Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Pseudomonas Aeruginosa Rmla in Complex with Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl1294 b:48.6 occ:1.00 ND1 D:HIS116 3.2 44.1 1.0 O D:HOH2065 3.5 42.2 1.0 CA D:HIS116 3.9 41.0 1.0 O D:HOH2147 3.9 39.4 1.0 N D:ASP117 3.9 49.8 1.0 CG D:HIS116 4.0 40.9 1.0 CB D:HIS116 4.1 40.2 1.0 CE1 D:HIS116 4.2 42.1 1.0 C D:HIS116 4.5 44.9 1.0 O D:GLY115 4.7 36.3 1.0 N D:HIS116 4.9 36.7 1.0

M.S.Alphey, L.Pirrie, L.S.Torrie, W.A.Boulkeroua, M.Gardiner, A.Sarkar, M.Maringer, W.Oehlmann, R.Brenk, M.S.Scherman, M.Mcneil, M.Rejzek, R.A.Field, M.Singh, D.Gray, N.J.Westwood, J.H.Naismith. Allosteric Competitive Inhibitors of the Glucose-1-Phosphate Thymidylyltransferase (Rmla) From Pseudomonas Aeruginosa. Acs Chem. Biol. V. 8 387 2013.
ISSN: ESSN 1554-8937
PubMed: 23138692
DOI: 10.1021/CB300426U