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AlphaFold monomer V2.0 prediction for peptidase E (Q4QMU5)

Analyse AlphaFold monomer V2.0 prediction for peptidase E (Q4QMU5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q4QMU5
Type
protein
Length
234 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x5f589287314FcB5B87F1F71E7db97a0D3F14CeaE
Molecule
Peptidase E
UniProt
Q4QMU5
Pockets
1 · best druggability 0.30

Structure

1 distinct chain · 32% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidase Eprotein23432% helix, 25% strandQ4QMU5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.300.7515empty

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