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AlphaFold monomer V2.0 prediction for rhomboid protease glpg (B5R383)

Analyse AlphaFold monomer V2.0 prediction for rhomboid protease glpg (B5R383) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B5R383
Type
protein
Length
276 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
Molecule
Rhomboid protease glpg
UniProt
B5R383
Pockets
2 · best druggability 0.42

Structure

1 distinct chain · 68% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARhomboid protease glpgprotein27668% helix, 6% strandB5R383

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.420.8312empty
2890.410.7812empty

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