Crystal structure of the epsin N-terminal homology (ENTH) domain at 1.56 Å resolution. Determined by X-ray diffraction at 1.56 Å resolution. Released 7 Jun 2000.
Explore 1EYH in 3D Show helices and sheets RCSB PDB PDBe
1EYH contains 12 α-helices and 2 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 | 16-18 | 3 | |
| α-helix | 19-27 | 9 | |
| α-helix | 34-36 | 3 | |
| α-helix | 37-46 | 10 | |
| α-helix | 50-64 | 15 | |
| α-helix | 68-70 | 3 | |
| α-helix | 71-87 | 17 | |
| α-helix | 90-98 | 9 | |
| α-helix | 100-104 | 5 | |
| α-helix | 105-108 | 4 | |
| β-strand | 112 | 1 | 1 |
| β-strand | 118 | 1 | 1 |
| α-helix | 120-135 | 16 | |
| α-helix | 137-155 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epsin | A | protein | 144 | Rattus norvegicus | O88339 (AlphaFold model) |
>1EYH_1 EPSIN (chains A) HNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHV YKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALL RDEDRLREERAHALKTKEKLAQTA
CRYSTAL STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN AT 1.56 ANGSTROM RESOLUTION. FREMONT, D.H. To be published.
Other PDB entries of the same protein (UniProt O88339 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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