Research workbench

AlphaFold monomer V2.0 prediction for insulin-induced gene 2 protein (Q9Y5U4)

Analyse AlphaFold monomer V2.0 prediction for insulin-induced gene 2 protein (Q9Y5U4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q9Y5U4
Type: protein
Length: 225 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
UniProt: Q9Y5U4

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	225	—	Q9Y5U4

Compared structures

7ETW · Cryo-EM structure of SCAP/INSIG complex in the present of digitonin. · an experimental structure of the same protein · chain A against A, TM-score 0.76
7ETW · Cryo-EM structure of Scap/Insig complex in the present of digitonin. · an experimental structure of the same protein · chain A against A, TM-score 0.76
6M49 · Cryo-EM structure of SCAP/INSIG complex in the present of 25-hydroxyl cholesterol. · an experimental structure of the same protein · chain A against A, TM-score 0.74
6M49 · cryo-EM structure of Scap/Insig complex in the present of 25-hydroxyl cholesterol. · an experimental structure of the same protein · chain A against A, TM-score 0.74
4J82 · Crystal structure of beta'-COP/Insig-2 complex · an experimental structure of the same protein · chain A against C, TM-score 0.02
4J82 · Crystal structure of beta'-COP/INSIG-2 complex · an experimental structure of the same protein · chain A against C, TM-score 0.02

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 Q9Y5U4
Elsewhere: UniProt Q9Y5U4 · AlphaFold DB Q9Y5U4

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