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AlphaFold monomer V2.0 prediction for transmembrane protein 196 (Q5EB63)

Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 196 (Q5EB63) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q5EB63
Type
protein
Length
176 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xd1A2963012bEcbC7A8f505464439Ab678C48936f
Molecule
Transmembrane protein 196
UniProt
Q5EB63
Pockets
2 · best druggability 0.73

Structure

1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransmembrane protein 196protein17678% helix, 0% strandQ5EB63

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14640.730.8261empty
21130.420.7625empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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