Structure of the third EPS15 homology domain of human EPS15. Determined by solution NMR. Released 19 Jul 2000.
Explore 1C07 in 3D Show helices and sheets RCSB PDB PDBe
1C07 contains 5 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 | 15-27 | 13 | |
| β-strand | 34-35 | 2 | 1 |
| α-helix | 37-45 | 9 | |
| α-helix | 51-61 | 11 | |
| β-strand | 69-70 | 2 | 1 |
| α-helix | 74-85 | 12 | |
| α-helix | 101-102 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (epidermal growth factor receptor pathway substrate 15) | A | protein | 95 | Homo sapiens | P42566 (AlphaFold model) |
>1C07_1 PROTEIN (EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 15) (chains A) TWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGK LSKDQFALAFHLISQKLIKGIDPPHVLTPEMIPPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Solution structure of Eps15's third EH domain reveals coincident Phe-Trp and Asn-Pro-Phe binding sites. Enmon, J.L., de Beer, T., Overduin, M. Biochemistry (2000) 39:4309-4319. DOI 10.1021/bi9927383 · 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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