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AlphaFold monomer V2.0 prediction for S-formylglutathione hydrolase frmb (Q1RFI8)

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

Accession
Q1RFI8
Type
protein
Length
277 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
Molecule
S-formylglutathione hydrolase frmb
UniProt
Q1RFI8

Structure

1 distinct chain · 40% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-formylglutathione hydrolase frmbprotein27740% helix, 27% strandQ1RFI8

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