Platinum in PDB 4qot: Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion

All present enzymatic activity of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion:
3.6.3.54;

The structure of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot was solved by B.D.Belviso, A.Galliani, R.Caliandro, F.Arnesano, G.Natile, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.49 / 2.20
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	78.055, 78.055, 54.628, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 23.9

The binding sites of Platinum atom in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion (pdb code 4qot). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 2 binding sites of Platinum where determined in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot:
Jump to Platinum binding site number: 1; 2;

Platinum binding site 1 out of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt101 b:26.8 occ:0.40 SG B:CYS15 2.3 25.7 1.0 SG B:CYS12 2.3 24.0 1.0 SG A:CYS15 2.3 28.6 1.0 SG A:CYS12 2.3 22.8 1.0 CB A:CYS12 3.4 20.4 1.0 CB B:CYS12 3.5 19.2 1.0 CB A:CYS15 3.5 20.7 1.0 CB B:CYS15 3.6 19.9 1.0 N A:CYS15 3.6 21.0 1.0 N B:CYS12 3.7 31.1 1.0 N B:CYS15 3.7 19.5 1.0 N A:CYS12 4.0 29.5 1.0 CA A:CYS15 4.0 21.0 1.0 OG1 B:THR11 4.0 34.2 1.0 CA B:CYS15 4.0 22.0 1.0 CA B:CYS12 4.1 19.1 1.0 CA A:CYS12 4.1 21.4 1.0 OG1 A:THR11 4.4 21.7 1.0 C A:THR11 4.5 22.8 1.0 O A:CYS12 4.5 24.6 1.0 O B:CYS12 4.5 19.0 1.0 C B:CYS12 4.5 18.8 1.0 C A:CYS12 4.5 30.5 1.0 C A:GLY14 4.6 23.2 1.0 C B:GLY14 4.6 24.9 1.0 C B:THR11 4.7 22.7 1.0 N B:THR11 4.7 17.7 1.0 N A:THR11 4.9 25.1 1.0 O A:THR11 4.9 29.2 1.0 CA B:THR11 4.9 22.6 1.0 CA A:GLY14 5.0 22.0 1.0 CB B:THR11 5.0 22.3 1.0

Platinum binding site 2 out of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt101 b:49.6 occ:0.25 O1 B:SO4104 1.9 46.1 0.4 OE1 B:GLU5 2.1 52.0 0.4 NZ B:LYS3 2.1 39.4 0.3 OE2 B:GLU5 2.3 31.3 0.4 SG B:CYS41 2.4 30.2 0.4 CD B:GLU5 2.4 49.4 0.4 SG B:CYS41 2.8 61.5 0.6 CE B:LYS3 2.8 35.0 0.3 CB B:CYS41 3.2 4.6 0.6 S B:SO4104 3.2 47.5 0.4 CB B:CYS41 3.2 30.0 0.4 O2 B:SO4104 3.6 46.0 0.4 O3 B:SO4104 3.7 48.8 0.4 CG B:GLU5 3.8 51.7 0.4 CD B:LYS3 3.9 34.2 0.3 OE1 B:GLU5 4.1 35.0 0.6 CD B:GLU5 4.2 27.4 0.6 O4 B:SO4104 4.3 44.4 0.4 CA B:CYS41 4.4 39.4 0.4 OE2 B:GLU5 4.4 21.3 0.6 CA B:CYS41 4.5 10.1 0.6 CG B:GLU5 4.6 22.8 0.6 CB B:GLU5 4.7 19.2 0.6 CB B:GLU5 4.7 49.1 0.4 CG B:LYS3 4.8 32.7 0.3

B.D.Belviso, A.Galliani, A.Lasorsa, V.Mirabelli, R.Caliandro, F.Arnesano, G.Natile. Oxaliplatin Binding to Human Copper Chaperone ATOX1 and Protein Dimerization Inorg.Chem. V. 55 6563 2016.
ISSN: ISSN 0020-1669
PubMed: 27305454
DOI: 10.1021/ACS.INORGCHEM.6B00750