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AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B3EFN5)

Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B3EFN5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B3EFN5
Type
protein
Length
440 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xf0a76e0131e9a5A06d4C89fDa82CFFD57de1b97c
UniProt
B3EFN5

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein440—B3EFN5

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