MolNFT v1 · #46079 · protein

Structure of the glutathione transferase from ochrobactrum anthropi in complex with glutathione

2NTO · Glutathione S-transferase: “Structure of the glutathione transferase from ochrobactrum anthropi in complex with glutathione”. X-ray diffraction, 2 ligands (GSH, SO4), 1 pocket (best druggability 0.40). MolNFT v1 #46079 on GenesisL1…

PDB: 2NTO
Type: protein
Length: 201 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
EC: 2.5.1.18
UniProt: P81065
Ligands: GSH, SO4
Pockets: 1 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione S-transferase (EC 2.5.1.18)	protein	201	53% helix, 11% strand	P81065

Ligands and binding sites

GSH · Glutathione · ligand · chains A
SO4 · Sulfate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.40	0.75	24	GSH

Compared structures

2NTO · Structure of the Glutathione Transferase from Ochrobactrum anthropi in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
P81065 · AlphaFold monomer V2.0 prediction for glutathione S-transferase (P81065) · a predicted model of the same protein · chain A 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 P81065
Elsewhere: RCSB PDB 2NTO · PDBe 2NTO · UniProt P81065

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