Structure of the second EPS15 homology domain of human EPS15, NMR, 20 structures. Determined by solution NMR. Released 22 Jul 1999.
Explore 1EH2 in 3D Show helices and sheets RCSB PDB PDBe
1EH2 contains 4 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 | 11-21 | 11 | |
| β-strand | 32 | 1 | 1 |
| α-helix | 33-41 | 9 | |
| α-helix | 47-57 | 11 | |
| β-strand | 64 | 1 | 1 |
| α-helix | 67-82 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| EPS15 | A | protein | 106 | Homo sapiens | P42566 (AlphaFold model) |
>1EH2_1 EPS15 (chains A) NRWGSPWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDID HDGMLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWLEI
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. de Beer, T., Carter, R.E., Lobel-Rice, K.E. et al. Science (1998) 281:1357-1360. DOI 10.1126/science.281.5381.1357 · PubMed
Other PDB entries of the same protein (UniProt P42566 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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