Chlorine in PDB 5oc8: HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A

All present enzymatic activity of HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A:
2.3.2.27;

The structure of HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A, PDB code: 5oc8 was solved by J.Kallen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.21 / 1.56
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	56.406, 56.406, 104.913, 90.00, 90.00, 120.00
R / Rfree (%)	23.7 / 26

The binding sites of Chlorine atom in the HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A (pdb code 5oc8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A, PDB code: 5oc8:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:16.2 occ:1.00 CL2 A:9QW201 0.0 16.2 1.0 C18 A:9QW201 1.7 14.2 1.0 C19 A:9QW201 2.7 15.7 1.0 C17 A:9QW201 2.7 15.1 1.0 CD1 A:ILE61 3.7 14.1 1.0 CZ A:PHE86 3.7 15.5 1.0 CE2 A:PHE86 3.8 16.2 1.0 CB A:LEU57 3.8 14.5 1.0 CG2 A:ILE99 3.9 16.6 1.0 C20 A:9QW201 4.0 15.0 1.0 C16 A:9QW201 4.0 15.7 1.0 CD1 A:LEU57 4.2 16.1 1.0 CZ A:PHE91 4.4 18.6 1.0 CD1 A:ILE103 4.5 18.5 1.0 C13 A:9QW201 4.5 16.3 1.0 CE1 A:PHE91 4.6 19.0 1.0 CG A:LEU57 4.6 14.5 1.0 CD1 A:LEU54 4.7 17.6 0.5 C A:LEU57 4.7 13.9 1.0 N A:GLY58 4.8 14.2 1.0 O A:LEU57 4.9 13.5 1.0 CA A:LEU57 4.9 14.2 1.0 CG1 A:ILE103 5.0 17.5 1.0

Chlorine binding site 2 out of 3 in the HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:21.9 occ:1.00 CL3 A:9QW201 0.0 21.9 1.0 C24 A:9QW201 1.7 22.3 1.0 C23 A:9QW201 2.7 25.1 1.0 C25 A:9QW201 2.7 23.0 1.0 CG A:HIS96 3.5 23.5 1.0 CE1 A:TYR100 3.6 22.9 1.0 CB A:HIS96 3.7 23.0 1.0 CA A:HIS96 3.7 22.7 1.0 O A:HIS96 3.7 21.7 1.0 CD2 A:HIS96 3.7 24.3 1.0 CG2 A:ILE99 3.7 16.6 1.0 CB A:ILE99 3.8 17.7 1.0 CD1 A:LEU54 3.8 17.6 0.5 CZ A:TYR100 3.8 24.5 1.0 N22 A:9QW201 3.9 26.9 1.0 CD2 A:LEU54 3.9 16.1 0.5 CD1 A:TYR100 3.9 23.9 1.0 C14 A:9QW201 4.0 23.2 1.0 ND1 A:HIS96 4.0 25.0 1.0 C A:HIS96 4.1 22.0 1.0 CD1 A:ILE99 4.2 19.2 1.0 OH A:TYR100 4.2 26.8 1.0 NE2 A:HIS96 4.3 24.5 1.0 CE1 A:HIS96 4.4 25.4 1.0 CE2 A:TYR100 4.4 23.6 1.0 C21 A:9QW201 4.5 26.4 1.0 CG A:TYR100 4.5 19.8 1.0 CG1 A:ILE99 4.6 18.8 1.0 CG A:LEU54 4.6 17.1 0.5 N A:TYR100 4.7 18.3 1.0 CD2 A:TYR100 4.8 20.7 1.0 N A:HIS96 4.9 23.1 1.0 CA A:ILE99 4.9 18.2 1.0

Chlorine binding site 3 out of 3 in the HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of HDM2 (17-111, Wild Type) Complexed with Nvp-HDM201 at 1.56A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:12.8 occ:0.50 O A:HOH335 2.9 24.0 1.0 N A:LEU81 3.2 15.0 1.0 NZ A:LYS64 3.3 12.8 1.0 OD1 A:ASP80 3.4 13.4 1.0 CG A:ASP80 3.6 12.4 1.0 CG A:LEU81 3.6 15.7 0.5 OH A:TYR60 3.7 13.5 1.0 CB A:LEU81 3.7 16.4 0.5 OD2 A:ASP80 3.8 12.8 1.0 CA A:ASP80 3.8 14.1 1.0 CB A:LEU81 4.0 15.3 0.5 C A:ASP80 4.0 14.4 1.0 CA A:LEU81 4.1 15.6 0.5 CA A:LEU81 4.2 15.2 0.5 CB A:ASP80 4.3 14.2 1.0 CD2 A:LEU81 4.5 15.0 0.5 CD1 A:LEU81 4.5 14.9 0.5 CE A:LYS64 4.8 12.2 1.0 O A:ASN79 4.8 17.1 1.0

S.Jeay, S.Ferretti, P.Holzer, J.Fuchs, E.A.Chapeau, M.Wartmann, D.Sterker, V.Romanet, M.Murakami, G.Kerr, E.Y.Durand, S.Gaulis, M.Cortes-Cros, S.Ruetz, T.M.Stachyra, J.Kallen, P.Furet, J.Wurthner, N.Guerreiro, E.Halilovic, A.Jullion, A.Kauffmann, E.Kuriakose, M.Wiesmann, M.R.Jensen, F.Hofmann, W.R.Sellers. Dose and Schedule Determine Distinct Molecular Mechanisms Underlying the Efficacy of the P53-MDM2 Inhibitor HDM201. Cancer Res. V. 78 6257 2018.
ISSN: ESSN 1538-7445
PubMed: 30135191
DOI: 10.1158/0008-5472.CAN-18-0338