9CC5: Amylin-NHO-22 Binder

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.

Method
X-ray diffraction
Resolution
1.87 Å
Organisms
synthetic construct, Homo sapiens
Chains
2
Atoms
1,332
Mol. weight
19.07 kDa
Released
14 May 2025

Explore 9CC5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 5 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand3-641
α-helix7-93
β-strand10-1231
α-helix17-4024
β-strand44-4741
α-helix50-6718
α-helix73-9826
β-strand104-114111
β-strand117-12481
α-helix126-1327
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix140-15617
β-strand159-16241

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amylin-NHO-22 BinderAprotein133synthetic construct
Islet amyloid polypeptideBprotein37Homo sapiensP10997 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9CC5_1 Amylin-NHO-22 Binder (chains A)
SLIVAVASPVVVAAHSPEDEERAEKEAERLRRRFAEELRKKGFEVVELDEETDEELRRWL
TKAIREATQAPTQEEFNQAVAEAIEKALERIEEIARRRHPDREVAAVLTVAVVHDGEVIA
TIFASPRLREALK
Sequence of entity 2 (B), FASTA
>9CC5_2 Islet amyloid polypeptide (chains B)
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Primary citation

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:

Browse structure collections

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