Zinc in PDB 8cg7: Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277

The structure of Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277, PDB code: 8cg7 was solved by D.I.Balourdas, M.M.Pichon, M.G.J.Baud, S.Knapp, A.C.Joerger, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.90 / 1.53
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	64.881, 71.046, 104.887, 90, 90, 90
R / Rfree (%)	15.8 / 18.7

The structure of Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277 also contains other interesting chemical elements:

Iodine

(I)

4 atoms

The binding sites of Zinc atom in the Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277 (pdb code 8cg7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277, PDB code: 8cg7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277


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 with Arylation at CYS182 and CYS277 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:22.2 occ:1.00 ND1 A:HIS179 2.0 19.1 1.0 SG A:CYS238 2.2 18.2 0.3 SG A:CYS176 2.3 19.7 1.0 SG A:CYS242 2.3 23.7 1.0 SG A:CYS238 2.4 21.4 0.7 CE1 A:HIS179 2.9 22.1 1.0 CG A:HIS179 3.0 20.2 1.0 CB A:CYS242 3.1 24.4 1.0 CB A:CYS238 3.3 20.2 0.7 CB A:CYS176 3.4 18.9 1.0 CB A:HIS179 3.5 18.9 1.0 CB A:CYS238 3.6 19.6 0.3 CA A:CYS238 3.8 19.2 0.3 CA A:CYS238 3.8 18.6 0.7 NE2 A:HIS179 4.0 21.9 1.0 N A:CYS176 4.1 19.7 1.0 CD2 A:HIS179 4.1 21.9 1.0 N A:TYR239 4.2 20.7 1.0 N A:HIS179 4.3 21.1 1.0 CA A:CYS176 4.3 19.3 1.0 CA A:HIS179 4.5 19.8 1.0 C A:CYS238 4.5 19.5 0.3 CA A:CYS242 4.5 22.4 1.0 C A:CYS238 4.6 19.4 0.7 O A:HOH591 4.7 25.3 1.0 O A:MET237 4.8 18.8 1.0 C A:CYS176 5.0 20.3 1.0

Zinc binding site 2 out of 2 in the Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of P53 Cancer Mutant Y220C with Arylation at CYS182 and CYS277 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:21.5 occ:1.00 ND1 B:HIS179 2.0 22.3 1.0 SG B:CYS176 2.3 19.2 1.0 SG B:CYS238 2.3 28.2 1.0 SG B:CYS242 2.3 24.7 1.0 CE1 B:HIS179 2.9 23.9 1.0 CG B:HIS179 3.1 21.5 1.0 CB B:CYS242 3.1 22.4 1.0 CB B:CYS176 3.3 18.6 1.0 CB B:CYS238 3.5 23.2 1.0 CB B:HIS179 3.5 18.6 1.0 CA B:CYS238 3.9 20.4 1.0 N B:CYS176 4.0 17.6 1.0 NE2 B:HIS179 4.1 24.3 1.0 CD2 B:HIS179 4.2 23.6 1.0 N B:HIS179 4.3 20.7 1.0 CA B:CYS176 4.3 18.4 1.0 N B:TYR239 4.3 20.8 1.0 CA B:HIS179 4.5 19.0 1.0 CA B:CYS242 4.5 22.6 1.0 C B:CYS238 4.6 21.4 1.0 O B:HOH597 4.8 22.0 1.0 O B:MET237 4.8 18.7 1.0 C B:CYS176 5.0 19.2 1.0

M.M.Pichon, D.Drelinkiewicz, D.Lozano, R.Moraru, L.J.Hayward, M.Jones, M.A.Mccoy, S.Allstrum-Graves, D.I.Balourdas, A.C.Joerger, R.J.Whitby, S.M.Goldup, N.Wells, G.J.Langley, J.M.Herniman, M.G.J.Baud. Structure-Reactivity Studies of 2-Sulfonylpyrimidines Allow Selective Protein Arylation. Bioconjug.Chem. V. 34 1679 2023.
ISSN: ISSN 1043-1802
PubMed: 37657082
DOI: 10.1021/ACS.BIOCONJCHEM.3C00322