MolNFT v1 · #176736 · protein

Crystal structure of a glutathione S-transferase SBGSTU6 from salix babylonica in complex with glutathione

7DW1: “Crystal structure of a glutathione S-transferase SBGSTU6 from salix babylonica in complex with glutathione”. X-ray diffraction, 1 ligand (GSH), 3 pockets (best druggability 0.67). MolNFT v1 #176736 on GenesisL1: 3D structure…

PDB: 7DW1
Type: protein
Length: 436 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione S-transferase
UniProt: A0A4Y5R032
Ligands: GSH
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glutathione S-transferase	protein	218	54% helix, 6% strand	A0A4Y5R032

Ligands and binding sites

GSH · Glutathione · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	872	0.67	0.73	59	empty
2	302	0.55	0.75	38	GSH
3	257	0.50	0.74	30	GSH

Interfaces

1 interface between chains.

A–B · 218 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7DW1 · Crystal structure of a glutathione S-transferase SbGSTU6 from Salix babylonica in complex… · the same entry in another collection · 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 A0A4Y5R032
Elsewhere: RCSB PDB 7DW1 · PDBe 7DW1 · UniProt A0A4Y5R032

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