Research workbench

Drosophila thioredoxin, oxidized, P21

Analyse Drosophila thioredoxin, oxidized, P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XW9
Type: protein
Length: 424 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin
UniProt: Q9V429
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Thioredoxin	protein	106	41% helix, 26% strand	Q9V429

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.37	0.74	21	empty
2	53	0.26	0.73	13	empty

Interfaces

3 interfaces between chains.

C–D · 102 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 51 Å² buried · 0 hydrogen bonds · protein-protein
B–D · 45 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1XW9 · Drosophila thioredoxin, oxidized, P21 · the same entry in another collection · chain A against A, TM-score 1.00
Q9V429 · AlphaFold monomer V2.0 prediction for thioredoxin-2 (Q9V429) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9V429
Elsewhere: RCSB PDB 1XW9 · PDBe 1XW9 · UniProt Q9V429

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