MolNFT v1 · #137860 · protein

Echinococcus granulosus thioredoxin glutathione reductas (egtgr)

5W1J · Thioredoxin glutathione reductase: “Echinococcus granulosus thioredoxin glutathione reductas (egtgr)”. X-ray diffraction, 1 ligand (FAD), 14 pockets (best druggability 0.81). MolNFT v1 #137860 on GenesisL1: 3D structure, binding…

PDB: 5W1J
Type: protein
Length: 1,168 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin glutathione reductase
UniProt: Q869D7
Ligands: FAD
Pockets: 14 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thioredoxin glutathione reductase	protein	584	35% helix, 25% strand	Q869D7

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	862	0.81	0.83	104	FAD
2	821	0.80	0.83	107	FAD
3	983	0.77	0.79	73	empty
4	132	0.74	0.93	36	empty
5	702	0.71	0.78	51	empty

Interfaces

1 interface between chains.

A–B · 3849 Å² buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5W1J · Echinococcus granulosus thioredoxin glutathione reductas (egTGR) · 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 Q869D7
Elsewhere: RCSB PDB 5W1J · PDBe 5W1J · UniProt Q869D7

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