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AlphaFold monomer V2.0 prediction for phosphatidylserine decarboxylase proenzyme (C6E524)

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
C6E524
Type
protein
Length
219 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
Molecule
Phosphatidylserine decarboxylase proenzyme
UniProt
C6E524

Structure

1 distinct chain · 21% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhosphatidylserine decarboxylase proenzymeprotein21921% helix, 36% strandC6E524

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