Zinc in PDB 2bim: Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H

The structure of Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H, PDB code: 2bim was solved by A.C.Joerger, A.R.Fersht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.6 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.455, 70.992, 104.669, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22.3

The binding sites of Zinc atom in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H (pdb code 2bim). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H, PDB code: 2bim:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1291 b:16.2 occ:1.00 ND1 A:HIS179 2.1 5.0 1.0 SG A:CYS242 2.3 13.9 1.0 SG A:CYS238 2.4 13.2 1.0 SG A:CYS176 2.4 13.8 1.0 CG A:HIS179 3.0 8.3 1.0 CE1 A:HIS179 3.0 13.1 1.0 CB A:CYS242 3.1 14.4 1.0 CB A:CYS238 3.3 12.2 1.0 CB A:HIS179 3.4 10.3 1.0 CB A:CYS176 3.5 13.9 1.0 CA A:CYS238 3.8 9.3 1.0 N A:CYS176 4.0 12.3 1.0 O A:HOH2103 4.0 33.2 1.0 NE2 A:HIS179 4.2 9.9 1.0 CD2 A:HIS179 4.2 13.2 1.0 N A:HIS179 4.3 14.2 1.0 CA A:CYS176 4.3 15.5 1.0 N A:TYR239 4.4 10.2 1.0 CA A:HIS179 4.5 11.0 1.0 CA A:CYS242 4.5 17.4 1.0 O A:MET237 4.6 9.0 1.0 O A:HOH2091 4.6 14.3 1.0 C A:CYS238 4.6 11.0 1.0 N A:CYS238 5.0 9.8 1.0

Zinc binding site 2 out of 2 in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273H within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1291 b:15.6 occ:1.00 ND1 B:HIS179 2.1 11.6 1.0 SG B:CYS242 2.3 13.1 1.0 SG B:CYS176 2.4 10.8 1.0 SG B:CYS238 2.4 11.7 1.0 CE1 B:HIS179 3.0 15.1 1.0 CG B:HIS179 3.0 14.6 1.0 CB B:CYS242 3.1 8.4 1.0 CB B:CYS238 3.4 8.6 1.0 CB B:HIS179 3.4 12.1 1.0 CB B:CYS176 3.5 16.5 1.0 CA B:CYS238 3.8 10.5 1.0 N B:CYS176 4.0 14.7 1.0 O B:HOH2109 4.1 33.0 1.0 NE2 B:HIS179 4.1 13.6 1.0 CD2 B:HIS179 4.2 18.3 1.0 N B:HIS179 4.3 13.9 1.0 CA B:CYS176 4.3 14.5 1.0 N B:TYR239 4.4 8.7 1.0 CA B:CYS242 4.5 14.4 1.0 CA B:HIS179 4.5 10.4 1.0 O B:MET237 4.6 11.3 1.0 O B:HOH2095 4.6 11.8 1.0 C B:CYS238 4.7 11.5 1.0 N B:CYS238 5.0 8.9 1.0

A.C.Joerger, H.C.Ang, D.B.Veprintsev, C.M.Blair, A.R.Fersht. Structures of P53 Cancer Mutants and Mechanism of Rescue By Second-Site Suppressor Mutations J.Biol.Chem. V. 280 16030 2005.
ISSN: ISSN 0021-9258
PubMed: 15703170
DOI: 10.1074/JBC.M500179200