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AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (B4RMD5)

Analyse AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (B4RMD5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B4RMD5
Type
protein
Length
127 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
Molecule
Aspartate 1-decarboxylase
UniProt
B4RMD5

Structure

1 distinct chain · 14% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAspartate 1-decarboxylaseprotein12714% helix, 48% strandB4RMD5

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