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AlphaFold monomer V2.0 prediction for putative pterin-4-alpha- carbinolamine dehydratase (C1AMF4)

Analyse AlphaFold monomer V2.0 prediction for putative pterin-4-alpha- carbinolamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
C1AMF4
Type
protein
Length
94 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
Molecule
Putative pterin-4-alpha-carbinolamine dehydratase
UniProt
C1AMF4

Structure

1 distinct chain · 46% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative pterin-4-alpha-carbinolamine dehydrataseprotein9446% helix, 24% strandC1AMF4

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