Chlorine in PDB 8tab: Rta-PD00589

All present enzymatic activity of Rta-PD00589:
3.2.2.22;

The structure of Rta-PD00589, PDB code: 8tab was solved by M.J.Rudolph, N.Tumer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.83 / 2.26
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	169.146, 169.146, 55.913, 90, 90, 120
R / Rfree (%)	18.6 / 21.9

The binding sites of Chlorine atom in the Rta-PD00589 (pdb code 8tab). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Rta-PD00589, PDB code: 8tab:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Rta-PD00589


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Rta-PD00589 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:59.6 occ:1.00 O A:HOH506 2.4 47.3 1.0 NH1 A:ARG189 3.3 29.5 1.0 NH2 A:ARG189 3.9 31.4 1.0 CZ A:ARG189 4.1 31.3 1.0

Chlorine binding site 2 out of 3 in the Rta-PD00589


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Rta-PD00589 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:59.3 occ:1.00 NH2 A:ARG125 3.2 34.6 1.0 NE A:ARG125 3.4 33.5 1.0 CZ A:ARG125 3.8 36.9 1.0 O A:ALA118 3.8 43.1 1.0 CB A:PHE119 3.9 36.1 1.0 CA A:PHE119 4.0 35.2 1.0 C A:ALA118 4.1 45.8 1.0 N A:PHE119 4.2 34.9 1.0 CB A:ALA118 4.4 39.8 1.0 CD A:ARG125 4.7 33.0 1.0 O A:HOH503 4.9 47.5 1.0 CA A:ALA118 4.9 44.1 1.0

Chlorine binding site 3 out of 3 in the Rta-PD00589


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Rta-PD00589 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:63.9 occ:1.00 O A:HOH535 3.1 47.7 1.0 NH2 A:ARG114 3.5 34.7 1.0 NE A:ARG114 3.5 38.6 1.0 O A:HOH436 3.5 35.2 1.0 O A:HOH465 3.5 45.0 1.0 CE1 A:PHE92 3.8 38.5 1.0 CZ A:ARG114 3.9 40.0 1.0 CD1 A:PHE92 4.0 37.1 1.0 CG2 A:THR105 4.2 35.8 1.0 CD1 A:ILE104 4.3 36.8 1.0 CG1 A:ILE104 4.3 36.1 1.0 CA A:THR105 4.4 39.5 1.0 O A:ILE104 4.4 32.5 1.0 N A:THR105 4.5 31.8 1.0 OG1 A:THR116 4.6 37.4 1.0 C A:ILE104 4.6 36.9 1.0 CD A:ARG114 4.6 36.9 1.0 CZ A:PHE92 4.6 39.0 1.0 CB A:ARG114 4.7 31.3 1.0 O A:HOH463 4.8 40.8 1.0 CB A:THR105 4.8 40.5 1.0 CG A:PHE92 4.8 41.9 1.0

M.J.Rudolph, A.Dutta, A.M.Tsymbal, J.E.Mclaughlin, Y.Chen, S.A.Davis, S.A.Theodorous, M.Pierce, B.Algava, X.Zhang, Z.Szekely, J.Y.Roberge, X.P.Li, N.E.Tumer. Structure-Based Design and Optimization of A New Class of Small Molecule Inhibitors Targeting the P-Stalk Binding Pocket of Ricin. Bioorg.Med.Chem. V. 100 17614 2024.
ISSN: ESSN 1464-3391
PubMed: 38340640
DOI: 10.1016/J.BMC.2024.117614