structure of DYNA_1b7. Determined by X-ray diffraction at 3.15 Å resolution. Released 13 Aug 2025.
Explore 9CCE in 3D Show helices and sheets RCSB PDB PDBe
9CCE contains 19 α-helices and 0 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 4-25 | 22 | |
| α-helix | 29-51 | 23 | |
| α-helix | 55-76 | 22 | |
| α-helix | 80-94 | 15 | |
| α-helix | 101-122 | 22 | |
| α-helix | 129-139 | 11 | |
| α-helix | 146-163 | 18 | |
| α-helix | 170-179 | 10 | |
| α-helix | 184-196 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-26 | 20 | |
| α-helix | 30-51 | 22 | |
| α-helix | 55-75 | 21 | |
| α-helix | 80-95 | 16 | |
| α-helix | 101-122 | 22 | |
| α-helix | 128-139 | 12 | |
| α-helix | 146-163 | 18 | |
| α-helix | 168-179 | 12 | |
| α-helix | 186-198 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-10 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DYNA_1b7 | A, B | protein | 217 | synthetic construct | |
| Dynorphin A(1-17) | C, D | protein | 17 | Homo sapiens | P01213 (AlphaFold model) |
>9CCE_1 DYNA_1b7 (chains A, B) MSGKEEEIEKEFEEKKKIIEENLKEAEEEGEEEAAEKLKEALKKLEEAIKLHREGANPVE VELEEVTAIILNNLAVLLREGEEELAKELEKAIKLLEEKKDAPEEERLKAIAIAIIRSVL VLIKWEGGKDEETIEEIEEILENRENLSLEELREAYVRAEIAYLIESGIDPEAAKKVREK YERGAPLEELLKDIEKIEKEAKKREEEKKGSHHHHHH
>9CCE_2 Dynorphin A(1-17) (chains C, D) YGGFLRRIRPKLKWDNQ
Design of intrinsically disordered region binding proteins. Wu, K., Jiang, H., Hicks, D.R. et al. Science (2025) 389:eadr8063-eadr8063. DOI 10.1126/science.adr8063 · PubMed
Other PDB entries of the same protein (UniProt P01213 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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