Research workbench

Structure of thioredoxin reductase from the thermophilic eubacterium thermosipho africanus TCF52B

Analyse Structure of thioredoxin reductase from the thermophilic eubacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7JYP
Type: protein
Length: 305 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase
EC: 1.8.1.9
UniProt: B7ICV3
Ligands: FAD, NAD
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase (EC 1.8.1.9)	protein	305	27% helix, 31% strand	B7ICV3

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
NAD · Nicotinamide-adenine-dinucleotide · ligand · 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	769	0.78	0.82	81	FAD

Compared structures

7JYP · Structure of thioredoxin reductase from the thermophilic eubacterium Thermosipho… · 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 B7ICV3
Elsewhere: RCSB PDB 7JYP · PDBe 7JYP · UniProt B7ICV3

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