Chlorine in PDB 5ln2: Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument

The structure of Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument, PDB code: 5ln2 was solved by J.Kallen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.51 / 1.58
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	56.540, 56.540, 103.953, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 24.7

The binding sites of Chlorine atom in the Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument (pdb code 5ln2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument, PDB code: 5ln2:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:16.4 occ:1.00 CL1 A:6ZT201 0.0 16.4 1.0 C2 A:6ZT201 1.7 17.1 1.0 C9 A:6ZT201 2.7 17.6 1.0 C3 A:6ZT201 2.7 17.2 1.0 CE2 A:TYR100 3.6 13.8 1.0 CG2 A:ILE99 3.7 11.6 1.0 CG A:HIS96 3.7 15.7 1.0 O A:HIS96 3.8 14.9 1.0 CB A:HIS96 3.8 15.3 1.0 CA A:HIS96 3.8 15.2 1.0 CD2 A:TYR100 3.8 13.2 1.0 CD1 A:LEU54 3.8 13.0 1.0 CB A:ILE99 3.9 11.9 1.0 CD2 A:HIS96 3.9 15.9 1.0 C7 A:6ZT201 4.0 18.3 1.0 C5 A:6ZT201 4.0 17.4 1.0 C A:HIS96 4.2 15.3 1.0 CD1 A:ILE99 4.3 12.3 1.0 ND1 A:HIS96 4.4 16.0 1.0 CD2 A:LEU54 4.4 13.6 1.0 CZ A:TYR100 4.4 14.0 1.0 C6 A:6ZT201 4.5 18.4 1.0 NE2 A:HIS96 4.6 16.1 1.0 CG1 A:ILE99 4.7 12.2 1.0 CG A:LEU54 4.7 12.8 1.0 CG A:TYR100 4.8 12.6 1.0 CE1 A:HIS96 4.8 16.0 1.0 OH A:TYR100 4.9 15.4 1.0 N A:TYR100 4.9 11.5 1.0 N A:HIS96 5.0 15.4 1.0

Chlorine binding site 2 out of 3 in the Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:14.2 occ:1.00 CL7 A:6ZT201 0.0 14.2 1.0 C66 A:6ZT201 1.7 14.1 1.0 C67 A:6ZT201 2.7 14.4 1.0 C64 A:6ZT201 2.7 13.8 1.0 CB A:LEU57 3.8 10.1 1.0 CD1 A:ILE61 3.8 9.5 1.0 CZ A:PHE86 3.9 12.9 1.0 CG2 A:ILE99 3.9 11.6 1.0 CE2 A:PHE86 4.0 13.1 1.0 C69 A:6ZT201 4.0 14.5 1.0 C63 A:6ZT201 4.0 14.2 1.0 CD1 A:LEU57 4.4 11.3 1.0 CD1 A:ILE103 4.5 12.5 1.0 C62 A:6ZT201 4.5 14.5 1.0 CZ A:PHE91 4.6 12.3 1.0 CG A:LEU57 4.6 10.7 1.0 C A:LEU57 4.6 9.4 1.0 CD1 A:LEU54 4.7 13.0 1.0 CE1 A:PHE91 4.7 12.3 1.0 N A:GLY58 4.7 9.5 1.0 CA A:LEU57 4.8 9.6 1.0 O A:LEU57 4.9 9.1 1.0

Chlorine binding site 3 out of 3 in the Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:16.9 occ:0.50 O A:HOH351 2.9 26.7 1.0 N A:LEU81 3.3 14.1 1.0 OD1 A:ASP80 3.5 12.3 1.0 CA A:ASP80 3.6 14.0 1.0 NZ A:LYS64 3.7 12.5 1.0 CG A:ASP80 3.8 12.7 1.0 C A:ASP80 4.0 14.1 1.0 OD2 A:ASP80 4.2 12.6 1.0 CB A:LEU81 4.2 15.9 1.0 O A:ASN79 4.2 15.9 1.0 CB A:ASP80 4.3 13.2 1.0 CA A:LEU81 4.3 14.5 1.0 OH A:TYR60 4.5 9.9 1.0 N A:ASP80 4.7 14.8 1.0 C A:ASN79 4.9 15.5 1.0

P.Furet, K.Masuya, J.Kallen, T.Stachyra-Valat, S.Ruetz, V.Guagnano, P.Holzer, R.Mah, S.Stutz, A.Vaupel, P.Chene, S.Jeay, A.Schlapbach. Discovery of A Novel Class of Highly Potent Inhibitors of the P53-MDM2 Interaction By Structure-Based Design Starting From A Conformational Argument. Bioorg.Med.Chem.Lett. V. 26 4837 2016.
ISSN: ESSN 1464-3405
PubMed: 27542305
DOI: 10.1016/J.BMCL.2016.08.010