Zinc in PDB 2j21: Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R282W

The structure of Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R282W, PDB code: 2j21 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)	29.2 / 1.6
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.813, 71.398, 104.978, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 22.4

The binding sites of Zinc atom in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R282W (pdb code 2j21). 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-R282W, PDB code: 2j21:
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-R282W


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-R282W within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1289 b:26.3 occ:1.00 ND1 A:HIS179 2.0 13.9 1.0 SG A:CYS238 2.2 11.9 0.5 SG A:CYS176 2.3 15.4 1.0 SG A:CYS242 2.3 19.1 1.0 SG A:CYS238 2.4 13.8 0.5 CE1 A:HIS179 2.9 16.3 1.0 CB A:CYS242 3.1 18.6 1.0 CG A:HIS179 3.1 15.1 1.0 CB A:CYS176 3.4 15.9 1.0 CB A:HIS179 3.5 16.0 1.0 CB A:CYS238 3.5 17.4 0.5 CB A:CYS238 3.6 18.3 0.5 CA A:CYS238 3.9 14.5 0.5 CA A:CYS238 3.9 14.8 0.5 O A:HOH2096 3.9 35.7 1.0 N A:CYS176 4.0 13.2 1.0 NE2 A:HIS179 4.1 16.4 1.0 N A:TYR239 4.1 13.4 1.0 CD2 A:HIS179 4.2 16.3 1.0 N A:HIS179 4.3 16.9 1.0 CA A:CYS176 4.3 15.9 1.0 CA A:HIS179 4.5 16.4 1.0 C A:CYS238 4.5 15.0 1.0 CA A:CYS242 4.5 18.2 1.0 O A:HOH2081 4.8 25.9 1.0 O A:MET237 4.9 14.7 1.0 C A:CYS176 5.0 15.2 1.0

Zinc binding site 2 out of 2 in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R282W


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-R282W within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1290 b:29.3 occ:1.00 ND1 B:HIS179 2.1 18.9 1.0 SG B:CYS238 2.3 13.5 0.4 SG B:CYS176 2.3 16.4 1.0 SG B:CYS242 2.4 22.0 1.0 SG B:CYS238 2.4 13.3 0.6 CE1 B:HIS179 3.0 20.6 1.0 CB B:CYS242 3.1 19.1 1.0 CG B:HIS179 3.1 16.7 1.0 CB B:CYS176 3.4 16.4 1.0 CB B:HIS179 3.5 17.0 1.0 CB B:CYS238 3.5 18.3 0.6 CB B:CYS238 3.6 18.3 0.4 CA B:CYS238 3.8 17.0 0.4 CA B:CYS238 3.8 16.9 0.6 O B:HOH2096 3.9 36.5 1.0 N B:CYS176 4.0 13.6 1.0 NE2 B:HIS179 4.1 20.9 1.0 CD2 B:HIS179 4.2 21.0 1.0 N B:TYR239 4.2 17.2 1.0 N B:HIS179 4.3 19.0 1.0 CA B:CYS176 4.3 14.9 1.0 CA B:HIS179 4.5 17.0 1.0 CA B:CYS242 4.5 20.3 1.0 C B:CYS238 4.6 17.4 1.0 O B:HOH2083 4.7 22.0 1.0 O B:MET237 4.8 16.6 1.0 C B:CYS176 5.0 17.6 1.0

A.C.Joerger, H.C.Ang, A.R.Fersht. Structural Basis For Understanding Oncogenic P53 Mutations and Designing Rescue Drugs. Proc.Natl.Acad.Sci.Usa V. 103 15056 2006.
ISSN: ISSN 0027-8424
PubMed: 17015838
DOI: 10.1073/PNAS.0607286103