MolNFT v1 · #5330 · protein

Glutathione transferase from homo sapiens

1EEM · Glutathione-S-transferase: “Glutathione transferase from homo sapiens”. X-ray diffraction, 2 ligands (GSH, SO4), 1 pocket (best druggability 0.52). MolNFT v1 #5330 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EEM
Type: protein
Length: 237 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione-S-transferase
UniProt: P78417
Ligands: GSH, SO4
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione-S-transferase	protein	237	52% helix, 9% strand	P78417

Ligands and binding sites

GSH · Glutathione · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.52	0.77	23	GSH

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1EEM · Glutathione transferase from homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
P78417 · AlphaFold monomer V2.0 prediction for glutathione S-transferase omega-1 (P78417) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P78417
Elsewhere: RCSB PDB 1EEM · PDBe 1EEM · UniProt P78417

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