Research workbench

Structure of WT Human Glutathione Transferase in complex with cisplatin in the presence of glutathione.

Analyse Structure of WT Human Glutathione Transferase in complex with cisplatin in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DJL
Type: protein
Length: 419 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.8
Source: Homo sapiens
Molecule: Glutathione S-transferase P
EC: 2.5.1.18
UniProt: P09211
Ligands: GSH, PT, CA, CO3, SO4
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · resolution 1.8 · 2 distinct chains · 62% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase P (EC 2.5.1.18)	protein	210	62% helix, 8% strand	P09211
B	Glutathione S-transferase P (EC 2.5.1.18)	protein	209	61% helix, 9% strand	P09211

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B
PT · Platinum (II) ion · metal · 3 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains B
CO3 · Carbonate ion · ion · chains B
SO4 · Sulfate ion · ion · chains B
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	690	0.72	0.79	88	PT, GSH
2	101	0.38	0.75	18	empty
3	64	0.32	0.75	14	empty
4	63	0.29	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 1300 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5DJL · Structure of wt human glutathione transferase in complex with cisplatin in the presence… · the same entry in another collection · chain A against A, TM-score 1.00
P09211 · AlphaFold monomer V2.0 prediction for glutathione S-transferase P (P09211) · a predicted model of the same protein · chain B against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P09211
Elsewhere: RCSB PDB 5DJL · PDBe 5DJL · UniProt P09211

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.