MolNFT v1 · #136617 · protein
AlphaFold monomer V2.0 prediction for follistatin (P21674)
P21674: “AlphaFold monomer V2.0 prediction for follistatin (P21674)”. MolNFT v1 #136617 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P21674
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- UniProt
- P21674
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 344 | — | 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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P21674
- Elsewhere: UniProt P21674 · AlphaFold DB P21674
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