Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological PH solutions. Determined by solution NMR. Released 31 Jan 1994.
Explore 1EPH in 3D Show helices and sheets RCSB PDB PDBe
1EPH contains 0 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 | 19-21 | 3 | 1 |
| β-strand | 30-32 | 3 | 1 |
| β-strand | 34 | 1 | 2 |
| β-strand | 37 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor | A | protein | 53 | Mus musculus | P01132 (AlphaFold model) |
>1EPH_1 EPIDERMAL GROWTH FACTOR (chains A) NSYPGCPSSYDGYCLNGGVCMHIESLDSYTCNCVIGYSGDRCQTRDLRWWELR
Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions. Kohda, D., Inagaki, F. Biochemistry (1992) 31:11928-11939. DOI 10.1021/bi00162a036 · PubMed
Other PDB entries of the same protein (UniProt P01132 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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