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 / R_free (%)*	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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy