Zinc in PDB 8qwn: Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form)

The structure of Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form), PDB code: 8qwn was solved by D.I.Balourdas, S.Knapp, A.C.Joerger, Structural Genomics Consortium(Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.30 / 1.44
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	45.33, 45.33, 332.64, 90, 90, 120
R / Rfree (%)	16.9 / 20.9

The structure of Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form) also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Zinc atom in the Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form) (pdb code 8qwn). 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 Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form), PDB code: 8qwn:

Zinc binding site 1 out of 1 in the Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of P53 Cancer Mutant Y220C (Hexagonal Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:29.0 occ:1.00 ND1 A:HIS179 2.0 25.4 1.0 SG A:CYS238 2.2 20.3 0.6 SG A:CYS176 2.3 27.8 1.0 SG A:CYS242 2.4 29.4 1.0 SG A:CYS238 2.8 19.0 0.4 CE1 A:HIS179 2.9 27.5 1.0 CG A:HIS179 3.0 24.9 1.0 CB A:CYS242 3.1 28.9 1.0 CB A:CYS176 3.4 27.7 1.0 CB A:HIS179 3.4 25.8 1.0 CB A:CYS238 3.5 20.6 0.6 CB A:CYS238 3.7 22.3 0.4 CA A:CYS238 3.9 15.7 0.6 CA A:CYS238 3.9 18.2 0.4 NE2 A:HIS179 4.1 31.4 1.0 N A:TYR239 4.1 18.6 1.0 N A:CYS176 4.1 26.0 1.0 CD2 A:HIS179 4.1 30.5 1.0 N A:HIS179 4.3 30.3 1.0 CA A:CYS176 4.3 26.3 1.0 C A:CYS238 4.5 17.1 0.6 CA A:HIS179 4.5 26.5 1.0 C A:CYS238 4.5 17.8 0.4 CA A:CYS242 4.5 26.6 1.0 O A:CYS176 4.8 27.1 1.0 C A:CYS176 4.9 30.1 1.0 O A:TYR239 4.9 20.4 1.0 O A:MET237 4.9 19.4 1.0

D.I.Balourdas, A.M.Markl, A.Kramer, G.Settanni, A.C.Joerger. Structural Basis of P53 Inactivation By Cavity-Creating Cancer Mutations and Its Implications For the Development of Mutant P53 Reactivators. Cell Death Dis V. 15 408 2024.
ISSN: ISSN 2041-4889
PubMed: 38862470
DOI: 10.1038/S41419-024-06739-X