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AlphaFold monomer V2.0 prediction for thioredoxin 2 (P0AGG5)

Analyse AlphaFold monomer V2.0 prediction for thioredoxin 2 (P0AGG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P0AGG5
Type
protein
Length
139 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x26ca9158879e824EF8a73775708d1b19082345Fc
Molecule
Thioredoxin 2
UniProt
P0AGG5

Structure

1 distinct chain · 29% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThioredoxin 2protein13929% helix, 25% strandP0AGG5

Modifications

Observed in the structure: 1 disulfide (disulfide).

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