Zinc in PDB 2j20: Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273C

The structure of Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273C, PDB code: 2j20 was solved by A.C.Joerger, H.C.Ang, A.R.Fersht, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.4 / 1.8
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.720, 70.979, 105.184, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 20.6

The binding sites of Zinc atom in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273C (pdb code 2j20). 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-R273C, PDB code: 2j20:
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-R273C


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-R273C within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1291 b:19.1 occ:1.00 ND1 A:HIS179 2.0 12.7 1.0 SG A:CYS242 2.3 20.2 1.0 SG A:CYS238 2.4 24.9 1.0 SG A:CYS176 2.4 16.2 1.0 CE1 A:HIS179 2.9 17.0 1.0 CG A:HIS179 3.1 16.5 1.0 CB A:CYS242 3.1 18.2 1.0 CB A:HIS179 3.5 15.1 1.0 CB A:CYS176 3.5 15.3 1.0 CB A:CYS238 3.6 24.1 1.0 O A:HOH2095 3.9 33.3 1.0 CA A:CYS238 3.9 19.9 1.0 N A:CYS176 4.0 15.1 1.0 NE2 A:HIS179 4.1 17.4 1.0 CD2 A:HIS179 4.1 17.4 1.0 N A:TYR239 4.2 15.1 1.0 N A:HIS179 4.3 17.9 1.0 CA A:CYS176 4.3 16.1 1.0 CA A:HIS179 4.5 16.7 1.0 CA A:CYS242 4.6 21.1 1.0 C A:CYS238 4.6 16.6 1.0 O A:HOH2083 4.8 26.2 1.0 O A:MET237 4.8 14.6 1.0

Zinc binding site 2 out of 2 in the Human P53 Core Domain Mutant M133L-V203A-N239Y-N268D-R273C


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-R273C within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1291 b:19.5 occ:1.00 ND1 B:HIS179 2.1 15.4 1.0 SG B:CYS242 2.3 19.9 1.0 SG B:CYS238 2.4 20.9 1.0 SG B:CYS176 2.4 16.3 1.0 CE1 B:HIS179 3.0 17.8 1.0 CG B:HIS179 3.1 14.7 1.0 CB B:CYS242 3.1 17.3 1.0 CB B:CYS176 3.4 15.1 1.0 CB B:HIS179 3.4 13.8 1.0 CB B:CYS238 3.5 21.5 1.0 CA B:CYS238 3.8 17.0 1.0 O B:HOH2106 4.0 35.3 1.0 N B:CYS176 4.0 15.4 1.0 NE2 B:HIS179 4.1 16.5 1.0 CD2 B:HIS179 4.2 16.6 1.0 CA B:CYS176 4.3 16.0 1.0 N B:HIS179 4.3 18.0 1.0 N B:TYR239 4.3 14.7 1.0 CA B:HIS179 4.5 15.8 1.0 CA B:CYS242 4.6 20.6 1.0 C B:CYS238 4.6 14.5 1.0 O B:HOH2094 4.7 27.0 1.0 O B:MET237 4.7 16.5 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