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Crystal structure of mouse thioredoxin reductase type 2

Analyse Crystal structure of mouse thioredoxin reductase type 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZDL
Type: protein
Length: 484 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase 2, mitochondrial
EC: 1.8.1.9
UniProt: Q9JLT4
Ligands: FAD, NDP
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9)	protein	484	33% helix, 22% strand	Q9JLT4

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1168	0.79	0.80	121	FAD, NDP
2	324	0.64	0.80	36	empty
3	80	0.45	0.81	22	empty
4	75	0.32	0.74	18	empty
5	55	0.29	0.74	15	empty

Compared structures

1ZDL · Crystal Structure of Mouse Thioredoxin Reductase Type 2 · 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 Q9JLT4
Elsewhere: RCSB PDB 1ZDL · PDBe 1ZDL · UniProt Q9JLT4

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