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AlphaFold monomer V2.0 prediction for follistatin (P21674)

Analyse AlphaFold monomer V2.0 prediction for follistatin (P21674) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P21674
Type
protein
Length
344 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
UniProt
P21674

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein344—P21674

Compared structures

  • 2ARP · Activin a in complex with FS12 fragment of follistatin · an experimental structure of the same protein · chain A against F, TM-score 0.41
  • 2ARP · Activin A in complex with Fs12 fragment of follistatin · an experimental structure of the same protein · chain A against F, TM-score 0.41
  • 1LR7 · Crystal structure of FS1, the heparin-binding domain of follistatin, complexed with the… · an experimental structure of the same protein · chain A against A, TM-score 0.21
  • 1LR7 · Crystal structure of Fs1, the heparin-binding domain of follistatin, complexed with the… · an experimental structure of the same protein · chain A against A, TM-score 0.21
  • 1LR8 · Crystal structure of FS1, the heparin-binding domain of follistatin, complexed with the… · an experimental structure of the same protein · chain A against A, TM-score 0.21
  • 1LR8 · Crystal structure of Fs1, the heparin-binding domain of follistatin, complexed with the… · an experimental structure of the same protein · chain A against A, TM-score 0.21
  • 1LR9 · Structure of FS1, the heparin-binding domain of follistatin · an experimental structure of the same protein · chain A against A, TM-score 0.21
  • 1LR9 · STRUCTURE OF Fs1, THE HEPARIN-BINDING DOMAIN OF FOLLISTATIN · an experimental structure of the same protein · chain A against A, TM-score 0.21

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