MolNFT v2 · #216822 · protein

Thioredoxin glutathione reductase of Schistosoma mansoni fragment screen hit 19.

8PLI: “Thioredoxin glutathione reductase of Schistosoma mansoni fragment screen hit 19.”. X-ray diffraction at 2.33, 2 ligands (FAD, WZY), 15 pockets (best druggability 0.82). MolNFT v2 #216822 on GenesisL1: 3D structure, binding sites and…

PDB: 8PLI
Type: protein
Length: 1,173 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.33
Source: Schistosoma mansoni
Molecule: Thioredoxin glutathione reductase
EC: 1.6.4.5
UniProt: Q962Y6
Ligands: FAD, WZY
Pockets: 15 · best druggability 0.82

Structure

x-ray diffraction · resolution 2.33 · 2 distinct chains · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin glutathione reductase (EC 1.6.4.5)	protein	586	38% helix, 24% strand	Q962Y6
B	Thioredoxin glutathione reductase (EC 1.6.4.5)	protein	587	37% helix, 24% strand	Q962Y6

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
WZY · N-(4-methoxyphenyl)glycinamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1029	0.82	0.83	112	FAD
2	1047	0.82	0.83	111	FAD
3	233	0.56	0.78	39	empty
4	216	0.53	0.77	27	empty
5	89	0.45	0.80	22	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

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 Q962Y6
Elsewhere: RCSB PDB 8PLI · PDBe 8PLI · UniProt Q962Y6

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