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

Enzymatic activity of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence of Glutathione.

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

Protein crystallography data

The structure of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence of Glutathione., PDB code: 5djl 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) 29.18 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 77.450, 89.940, 68.780, 90.00, 98.03, 90.00
R / Rfree (%) 14.9 / 17.8

Other elements in 5djl:

The structure of Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence of Glutathione. also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Platinum Binding Sites:

The binding sites of Platinum atom in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence of Glutathione. (pdb code 5djl). 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 Presence of Glutathione., PDB code: 5djl:
Jump to Platinum binding site number: 1; 2; 3;

Platinum binding site 1 out of 3 in 5djl

Go back to Platinum Binding Sites List in 5djl
Platinum binding site 1 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence 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 Presence of Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt302

b:26.4
occ:0.30
 SG B:CYS101 2.3 22.3 0.5
O B:HOH644 2.4 26.1 0.7
SG A:CYS101 2.5 29.2 0.5
O A:HOH608 2.8 27.6 0.7
O B:HOH618 2.9 26.7 0.6
HB3 B:CYS101 3.0 22.5 0.5
O A:HOH582 3.0 41.1 1.0
HB3 A:CYS101 3.2 25.2 0.5
PT B:PT306 3.5 57.8 0.2
PT A:PT303 3.5 58.3 0.2
SG B:CYS101 3.6 12.2 0.5
CB B:CYS101 3.7 18.8 0.5
CB B:CYS101 3.7 18.8 0.5
SG A:CYS101 3.7 12.8 0.5
HG B:CYS101 3.7 14.7 0.5
HB3 B:CYS101 3.8 22.6 0.5
CB A:CYS101 3.8 21.0 0.5
CB A:CYS101 3.8 21.0 0.5
HB2 B:CYS101 3.9 22.6 0.5
HB3 A:CYS101 3.9 25.2 0.5
HB2 B:CYS101 4.0 22.5 0.5
HB2 A:CYS101 4.0 25.2 0.5
HB2 A:CYS101 4.1 25.2 0.5
O B:HOH599 4.2 37.6 1.0
O B:HOH471 4.3 22.9 1.0
O A:HOH513 4.7 24.2 1.0
O A:HOH577 4.7 37.0 1.0
HG A:CYS101 4.8 15.3 0.5

Platinum binding site 2 out of 3 in 5djl

Go back to Platinum Binding Sites List in 5djl
Platinum binding site 2 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence 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 Presence of Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt303

b:58.3
occ:0.20
 SG A:CYS101 2.3 29.2 0.5
O A:HOH531 2.4 24.1 0.7
SG A:CYS101 2.8 12.8 0.5
O B:HOH644 2.8 26.1 0.7
HB3 A:CYS101 3.2 25.2 0.5
O A:HOH411 3.2 31.6 1.0
HH21 A:ARG13 3.5 23.0 1.0
CB A:CYS101 3.5 21.0 0.5
PT A:PT302 3.5 26.4 0.3
CB A:CYS101 3.5 21.0 0.5
HA A:CYS101 3.5 26.3 0.5
HA A:CYS101 3.5 26.4 0.5
HB2 A:CYS101 3.6 25.2 0.5
HG A:CYS101 3.7 15.3 0.5
NH2 A:ARG13 4.0 19.1 1.0
HH22 A:ARG13 4.0 23.0 1.0
CA A:CYS101 4.1 21.9 0.5
O A:HOH582 4.1 41.1 1.0
CA A:CYS101 4.1 22.0 0.5
HB3 A:CYS101 4.3 25.2 0.5
HB2 A:CYS101 4.3 25.2 0.5
O B:HOH471 4.6 22.9 1.0
OE2 A:GLU97 4.7 17.7 1.0
HD12 A:ILE104 4.7 26.4 1.0
O A:CYS101 4.9 21.8 1.0
HB A:ILE104 4.9 20.2 1.0
C A:CYS101 4.9 19.3 1.0
O A:HOH433 5.0 27.8 1.0

Platinum binding site 3 out of 3 in 5djl

Go back to Platinum Binding Sites List in 5djl
Platinum binding site 3 out of 3 in the Structure of Wt Human Glutathione Transferase in Complex with Cisplatin in the Presence 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 Presence of Glutathione. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt306

b:57.8
occ:0.20
 HG B:CYS101 1.8 14.7 0.5
SG B:CYS101 2.3 22.3 0.5
O B:HOH566 2.5 22.3 0.7
O A:HOH608 2.7 27.6 0.7
O B:HOH552 2.8 24.7 1.0
SG B:CYS101 2.8 12.2 0.5
HB3 B:CYS101 3.1 22.5 0.5
HA B:CYS101 3.3 20.7 0.5
HA B:CYS101 3.3 20.7 0.5
CB B:CYS101 3.4 18.8 0.5
CB B:CYS101 3.4 18.8 0.5
PT A:PT302 3.5 26.4 0.3
HB2 B:CYS101 3.5 22.6 0.5
O B:HOH618 3.5 26.7 0.6
HH21 B:ARG13 3.6 24.2 1.0
CA B:CYS101 3.9 17.2 0.5
CA B:CYS101 3.9 17.2 0.5
HB3 B:CYS101 4.3 22.6 0.5
HH22 B:ARG13 4.3 24.2 1.0
NH2 B:ARG13 4.3 20.1 1.0
HB2 B:CYS101 4.3 22.5 0.5
O B:CYS101 4.5 16.7 1.0
HB B:ILE104 4.6 21.2 1.0
C B:CYS101 4.6 16.4 1.0
HD12 B:ILE104 4.6 27.8 1.0
O A:HOH513 4.7 24.2 1.0
HG21 B:ILE104 4.9 22.0 1.0
O B:HOH427 4.9 25.3 1.0
O B:HOH629 4.9 38.1 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: Thu Oct 10 11:32:43 2024

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