Platinum in PDB 5djm: Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione.

All present enzymatic activity of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione.:
2.5.1.18;

The structure of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione., PDB code: 5djm was solved by L.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.98 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.517, 90.130, 68.943, 90.00, 97.85, 90.00
R / Rfree (%)	20.7 / 24

The binding sites of Platinum atom in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione. (pdb code 5djm). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 3 binding sites of Platinum where determined in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione., PDB code: 5djm:
Jump to Platinum binding site number: 1; 2; 3;

Platinum binding site 1 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione.


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione. within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt302 b:38.2 occ:0.71 SG A:CYS101 2.3 41.9 1.0 SG B:CYS101 2.4 42.8 1.0 CB B:CYS101 3.3 35.8 1.0 HB3 B:CYS101 3.3 43.0 1.0 CB A:CYS101 3.3 36.7 1.0 HB2 B:CYS101 3.4 43.0 1.0 HB3 A:CYS101 3.4 44.0 1.0 HB2 A:CYS101 3.5 44.0 1.0 PT B:PT302 3.5 52.0 0.6 PT A:PT303 3.5 63.2 0.6 CA A:CYS101 4.7 35.4 1.0 CA B:CYS101 4.8 34.0 1.0 HA A:CYS101 4.8 42.4 1.0

Platinum binding site 2 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione.


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione. within 5.0Å range: probe atom residue distance (Å) B Occ A:Pt303 b:63.2 occ:0.63 SG A:CYS101 2.2 41.9 1.0 HA A:CYS101 3.1 42.4 1.0 CB A:CYS101 3.3 36.7 1.0 HB2 A:CYS101 3.4 44.0 1.0 PT A:PT302 3.5 38.2 0.7 CA A:CYS101 3.7 35.4 1.0 HH21 A:ARG13 3.8 57.7 1.0 HB3 A:CYS101 4.2 44.0 1.0 O A:CYS101 4.2 38.9 1.0 C A:CYS101 4.4 36.6 1.0 HD12 A:ILE104 4.4 48.7 1.0 HH22 A:ARG13 4.4 57.7 1.0 HB A:ILE104 4.4 50.6 1.0 NH2 A:ARG13 4.5 48.1 1.0 N A:CYS101 4.9 34.0 1.0 HG21 A:ILE104 4.9 52.6 1.0

Platinum binding site 3 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione.


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 3 of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Absence of Glutathione. within 5.0Å range: probe atom residue distance (Å) B Occ B:Pt302 b:52.0 occ:0.61 SG B:CYS101 2.2 42.8 1.0 HB2 B:CYS101 2.9 43.0 1.0 CB B:CYS101 3.0 35.8 1.0 HA B:CYS101 3.1 40.8 1.0 PT A:PT302 3.5 38.2 0.7 CA B:CYS101 3.6 34.0 1.0 HH21 B:ARG13 3.6 49.9 1.0 HB3 B:CYS101 3.9 43.0 1.0 HH22 B:ARG13 4.1 49.9 1.0 NH2 B:ARG13 4.2 41.6 1.0 O B:CYS101 4.4 35.8 1.0 C B:CYS101 4.5 35.0 1.0 HB B:ILE104 4.6 47.2 1.0 HD12 B:ILE104 4.7 49.2 1.0 N B:CYS101 4.7 30.0 1.0 HG21 B:ILE104 4.8 52.5 1.0

L.J.Parker, L.C.Italiano, N.C.Hancock, J.Aitken, H.H.Harris, G.Hansen, D.B.Ascher, C.J.Morton, M.W.Parker, M.Lo Bello. A Structure-Based Mechanism of Cisplatin Resistance Mediated By Glutathione Transferase P1-1 Proc.Natl.Acad.Sci.Usa 2019.
ISSN: ESSN 1091-6490