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Crystal structure of T. acidophilum thioredoxin reductase

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

PDB: 3CTY
Type: protein
Length: 609 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin reductase
UniProt: Q9HJI4
Ligands: FAD
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin reductase	protein	304	26% helix, 32% strand	Q9HJI4
B	Thioredoxin reductase	protein	305	27% helix, 30% strand	Q9HJI4

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

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	905	0.78	0.81	90	FAD
2	947	0.78	0.81	94	FAD
3	153	0.52	0.80	25	empty

Interfaces

1 interface between chains.

A–B · 1837 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3CTY · Crystal structure of T. acidophilum thioredoxin reductase · 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 Q9HJI4
Elsewhere: RCSB PDB 3CTY · PDBe 3CTY · UniProt Q9HJI4

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