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AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase (B5EFG4)

Analyse AlphaFold monomer V2.0 prediction for glutamate-1-semialdehyde 2,1-aminomutase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B5EFG4
Type
protein
Length
427 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x67Caacc81C91Ffe8C5b6E9623969278a00FCc789
UniProt
B5EFG4

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein427—B5EFG4

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