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AlphaFold monomer V2.0 prediction for beta-fibrinogenase (E0Y419)

Analyse AlphaFold monomer V2.0 prediction for beta-fibrinogenase (E0Y419) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
E0Y419
Type
protein
Length
257 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
Molecule
Beta-fibrinogenase
UniProt
E0Y419
Pockets
2 · best druggability 0.37

Structure

1 distinct chain · 12% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-fibrinogenaseprotein25712% helix, 30% strandE0Y419

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1890.370.7620empty
2510.250.7316empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

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