Type alpha transforming growth factor, NMR, 16 models without energy minimization. Determined by solution NMR. Released 17 Aug 1996.
Explore 1YUF in 3D Show helices and sheets RCSB PDB PDBe
1YUF contains 1 α-helix and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-15 | 4 | |
| β-strand | 22-24 | 3 | 1 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 39 | 1 | 2 |
| β-strand | 45 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor alpha | A | protein | 50 | Homo sapiens | P01135 (AlphaFold model) |
>1YUF_1 TRANSFORMING GROWTH FACTOR ALPHA (chains A) VVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLA
Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints. Moy, F.J., Li, Y.C., Rauenbuehler, P. et al. Biochemistry (1993) 32:7334-7353. DOI 10.1021/bi00080a003 · PubMed
Other PDB entries of the same protein (UniProt P01135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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