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AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (C1FPI8)

Analyse AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
C1FPI8
Type
protein
Length
295 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x93B835B47972632E65dc11270e23B6d8C9ef14a3
Molecule
Phosphatidylserine decarboxylase proenzyme
UniProt
C1FPI8
Pockets
4 · best druggability 0.67

Structure

1 distinct chain · 28% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphatidylserine decarboxylase proenzymeprotein29528% helix, 28% strandC1FPI8

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12690.670.8333empty
22710.650.8240empty
32490.560.7728empty
4690.340.7614empty

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