Zinc in PDB 2x0u: Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold

The structure of Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold, PDB code: 2x0u was solved by A.C.Joerger, J.L.Kaar, N.Basse, A.R.Fersht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.71 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.060, 71.140, 105.410, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 19.3

The binding sites of Zinc atom in the Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold (pdb code 2x0u). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold, PDB code: 2x0u:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1300 b:10.4 occ:1.00 ND1 A:HIS179 2.1 9.7 1.0 SG A:CYS238 2.2 7.3 0.3 SG A:CYS242 2.3 11.2 1.0 SG A:CYS176 2.3 8.7 1.0 SG A:CYS238 2.4 8.1 0.7 CE1 A:HIS179 3.0 8.4 1.0 CG A:HIS179 3.1 10.4 1.0 CB A:CYS242 3.1 11.6 1.0 CB A:CYS176 3.4 9.4 1.0 CB A:HIS179 3.4 9.3 1.0 CB A:CYS238 3.5 10.1 1.0 CA A:CYS238 3.8 8.5 1.0 N A:CYS176 4.0 8.0 1.0 O A:HOH2194 4.0 21.9 1.0 NE2 A:HIS179 4.1 10.1 1.0 CD2 A:HIS179 4.2 11.8 1.0 N A:HIS179 4.3 8.2 1.0 N A:TYR239 4.3 9.6 1.0 CA A:CYS176 4.3 8.2 1.0 CA A:HIS179 4.5 8.7 1.0 CA A:CYS242 4.5 9.3 1.0 C A:CYS238 4.6 11.8 1.0 O A:HOH2172 4.7 12.9 1.0 O A:MET237 4.8 7.4 1.0 C A:CYS176 5.0 8.4 1.0

Zinc binding site 2 out of 2 in the Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the P53 Core Domain Mutant Y220C Bound to A 2-Amino Substituted Benzothiazole Scaffold within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1300 b:9.7 occ:1.00 ND1 B:HIS179 2.0 11.4 1.0 SG B:CYS176 2.3 8.7 1.0 SG B:CYS242 2.3 9.7 1.0 SG B:CYS238 2.3 8.4 1.0 CE1 B:HIS179 3.0 10.1 1.0 CG B:HIS179 3.1 8.6 1.0 CB B:CYS242 3.1 9.5 1.0 CB B:CYS238 3.3 8.5 1.0 CB B:CYS176 3.4 9.2 1.0 CB B:HIS179 3.4 8.0 1.0 CA B:CYS238 3.8 5.9 1.0 O B:HOH2170 3.9 22.4 1.0 N B:CYS176 4.0 7.0 1.0 NE2 B:HIS179 4.1 10.6 1.0 CD2 B:HIS179 4.2 10.3 1.0 CA B:CYS176 4.3 9.4 1.0 N B:HIS179 4.3 9.3 1.0 N B:TYR239 4.5 8.9 1.0 CA B:CYS242 4.5 8.6 1.0 CA B:HIS179 4.5 8.3 1.0 O B:MET237 4.6 8.6 1.0 O B:HOH2153 4.7 10.9 1.0 C B:CYS238 4.7 9.5 1.0 N B:CYS238 5.0 7.3 1.0 C B:CYS176 5.0 8.9 1.0

N.Basse, J.L.Kaar, G.Settanni, A.C.Joerger, T.J.Rutherford, A.R.Fersht. Toward the Rational Design of P53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant. Chem.Biol. V. 17 46 2010.
ISSN: ISSN 1074-5521
PubMed: 20142040
DOI: 10.1016/J.CHEMBIOL.2009.12.011