De novo design of high-affinity protein binders to bio active peptide Amylin. Determined by X-ray diffraction at 1.87 Å resolution. Released 14 May 2025.
Explore 9CC5 in 3D Show helices and sheets RCSB PDB PDBe
9CC5 contains 6 α-helices and 6 β-strands across 2 chains. 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 | 3-6 | 4 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 1 |
| α-helix | 17-40 | 24 | |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 50-67 | 18 | |
| α-helix | 73-98 | 26 | |
| β-strand | 104-114 | 11 | 1 |
| β-strand | 117-124 | 8 | 1 |
| α-helix | 126-132 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 140-156 | 17 | |
| β-strand | 159-162 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amylin-NHO-22 Binder | A | protein | 133 | synthetic construct | |
| Islet amyloid polypeptide | B | protein | 37 | Homo sapiens | P10997 (AlphaFold model) |
>9CC5_1 Amylin-NHO-22 Binder (chains A) SLIVAVASPVVVAAHSPEDEERAEKEAERLRRRFAEELRKKGFEVVELDEETDEELRRWL TKAIREATQAPTQEEFNQAVAEAIEKALERIEEIARRRHPDREVAAVLTVAVVHDGEVIA TIFASPRLREALK
>9CC5_2 Islet amyloid polypeptide (chains B) KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY
Diffusing protein binders to intrinsically disordered proteins. Liu, C., Wu, K., Choi, H. et al. Nature (2025) 644:809-817. DOI 10.1038/s41586-025-09248-9 · PubMed
Other PDB entries of the same protein (UniProt P10997 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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