Zinc in PDB 2biq: Human P53 Core Domain Mutant T123A-M133L-H168R-V203A-N239Y- R249S-N268D

The structure of Human P53 Core Domain Mutant T123A-M133L-H168R-V203A-N239Y- R249S-N268D, PDB code: 2biq 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)	39.4 / 1.8
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	45.480, 45.480, 331.080, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / 25.5

The binding sites of Zinc atom in the Human P53 Core Domain Mutant T123A-M133L-H168R-V203A-N239Y- R249S-N268D (pdb code 2biq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human P53 Core Domain Mutant T123A-M133L-H168R-V203A-N239Y- R249S-N268D, PDB code: 2biq:

Zinc binding site 1 out of 1 in the Human P53 Core Domain Mutant T123A-M133L-H168R-V203A-N239Y- R249S-N268D


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 T123A-M133L-H168R-V203A-N239Y- R249S-N268D within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1291 b:28.3 occ:1.00 ND1 A:HIS179 2.0 24.9 1.0 SG A:CYS176 2.4 23.9 1.0 SG A:CYS242 2.4 29.4 1.0 SG A:CYS238 2.4 29.9 1.0 CE1 A:HIS179 3.0 24.7 1.0 CG A:HIS179 3.0 24.8 1.0 CB A:CYS242 3.1 28.7 1.0 CB A:HIS179 3.4 27.3 1.0 CB A:CYS176 3.4 26.4 1.0 CB A:CYS238 3.6 29.4 1.0 CA A:CYS238 3.9 23.5 1.0 N A:CYS176 4.1 22.8 1.0 NE2 A:HIS179 4.1 24.4 1.0 N A:TYR239 4.1 21.1 1.0 CD2 A:HIS179 4.1 27.1 1.0 N A:HIS179 4.3 25.2 1.0 CA A:CYS176 4.3 25.3 1.0 CA A:HIS179 4.5 27.6 1.0 C A:CYS238 4.5 27.2 1.0 CA A:CYS242 4.6 36.3 1.0 O A:HOH2047 4.7 27.4 1.0 O A:TYR239 4.9 24.6 1.0 O A:CYS176 4.9 25.4 1.0 C A:CYS176 4.9 26.6 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