Atomistry » Platinum » PDB 5djl-5t7l » 5djm
Atomistry »
  Platinum »
    PDB 5djl-5t7l »
      5djm »

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

Enzymatic activity of 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;

Protein crystallography data

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

Platinum Binding Sites:

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 5djm

Go back to Platinum Binding Sites List in 5djm
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 5djm

Go back to Platinum Binding Sites List in 5djm
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 5djm

Go back to Platinum Binding Sites List in 5djm
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

Reference:

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
Page generated: Wed Dec 16 02:05:14 2020

Last articles

Zn in 7M6U
Zn in 7NNG
Zn in 7NEE
Zn in 7NEU
Zn in 7M3K
Zn in 7KWD
Zn in 7KYH
Zn in 7KNG
Zn in 7KY2
Zn in 7KYF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy