The solution structure of human transforming growth factor alpha. Determined by solution NMR. Released 15 Apr 1993.
Explore 2TGF in 3D Show helices and sheets RCSB PDB PDBe
2TGF 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 |
|---|---|---|---|
| β-strand | 19-24 | 6 | 1 |
| α-helix | 25-27 | 3 | |
| β-strand | 29-34 | 6 | 1 |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 45-46 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor-alpha | A | protein | 50 | Homo sapiens | P01135 (AlphaFold model) |
>2TGF_1 TRANSFORMING GROWTH FACTOR-ALPHA (chains A) VVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLA
The solution structure of human transforming growth factor alpha. Harvey, T.S., Wilkinson, A.J., Tappin, M.J. et al. Eur J Biochem (1991) 198:555-562. DOI 10.1111/j.1432-1033.1991.tb16050.x · 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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