Type alpha transforming growth factor, NMR, 15 models after ECEPP/3 energy minimization. Determined by solution NMR. Released 17 Aug 1996.
Explore 1YUG in 3D Show helices and sheets RCSB PDB PDBe
1YUG contains 1 α-helix and 5 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 |
|---|---|---|---|
| β-strand | 5 | 1 | 1 |
| α-helix | 12-15 | 4 | |
| β-strand | 19-24 | 6 | 1 |
| β-strand | 29-34 | 6 | 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) |
>1YUG_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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