Solution structure and dynamics of the EGF/TGF-alpha chimera T1E. Determined by solution NMR. Released 7 Oct 2003.
Explore 1P9J in 3D Show helices and sheets RCSB PDB PDBe
1P9J contains 2 α-helices 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 | 21-25 | 5 | 1 |
| β-strand | 30-34 | 5 | 1 |
| α-helix | 35-36 | 2 | |
| β-strand | 39-40 | 2 | 2 |
| β-strand | 46-47 | 2 | 2 |
| α-helix | 48 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha) | A | protein | 54 | Homo sapiens | P01133 (AlphaFold model) |
>1P9J_1 chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha) (chains A) VVSHFNDCPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWEL
Structural Analysis of an Epidermal Growth Factor/Transforming Growth Factor-alpha Chimera with Unique ErbB Binding Specificity. Wingens, M., Walma, T., Van Ingen, H. et al. J Biol Chem (2003) 278:39114-39123. DOI 10.1074/jbc.M305603200 · PubMed
Other PDB entries of the same protein (UniProt P01133 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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