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AlphaFold monomer V2.0 prediction for endophilin-B1 (Q9Y371)

Analyse AlphaFold monomer V2.0 prediction for endophilin-B1 (Q9Y371) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q9Y371
Type
protein
Length
365 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x2e8Fbb947b0Bc2a2DB44100d3D43354e3aA89cEA
Molecule
Endophilin-B1
UniProt
Q9Y371
Pockets
1 · best druggability 0.62

Structure

1 distinct chain · 61% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndophilin-B1protein36561% helix, 8% strandQ9Y371

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14400.620.7636empty

Compared structures

  • 9G2W · Endophilin B1 dimer bound to nanodisc edge · an experimental structure of the same protein · chain A against A, TM-score 0.62
  • 9G2R · Endophilin B1 dimers bound to nanodiscs · an experimental structure of the same protein · chain A against E, TM-score 0.62
  • 9G2U · Endophilin B1 dimer bound to nanodisc center · an experimental structure of the same protein · chain A against B, TM-score 0.60
  • 6UPN · Endophilin B1 helical scaffold · an experimental structure of the same protein · chain A against f, TM-score 0.50

Analyse

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