Structure of the second EPS15 homology domain of human EPS15 in complex with ptgssstnpfl. Determined by solution NMR. Released 1 Nov 2000.
Explore 1FF1 in 3D Show helices and sheets RCSB PDB PDBe
1FF1 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 | 11-21 | 11 | |
| β-strand | 32 | 1 | 1 |
| α-helix | 33-41 | 9 | |
| α-helix | 47-55 | 9 | |
| β-strand | 64 | 1 | 1 |
| α-helix | 67-82 | 16 | |
| α-helix | 97-99 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epidermal growth factor receptor substrate 15 | A | protein | 95 | Homo sapiens | P42566 (AlphaFold model) |
| Ptgssstnpfl peptide | B | protein | 11 |
>1FF1_1 EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15 (chains A) PWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGML DRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKR
>1FF1_2 PTGSSSTNPFL PEPTIDE (chains B) PTGSSSTNPFL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Molecular mechanism of NPF recognition by EH domains. de Beer, T., Hoofnagle, A.N., Enmon, J.L. et al. Nat Struct Biol (2000) 7:1018-1022. DOI 10.1038/80924 · 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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