Cryo EM structure of KCa3.1_R355K_II/calmodulin channel in complex with rimtuzalcap. Determined by electron microscopy at 3.4 Å resolution. Released 1 Oct 2025.
Explore 9YDZ in 3D Show helices and sheets RCSB PDB PDBe
9YDZ contains 85 α-helices and 0 β-strands across 8 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 | 10-50 | 41 | |
| α-helix | 56-72 | 17 | |
| α-helix | 76-91 | 16 | |
| α-helix | 96-99 | 4 | |
| α-helix | 102-115 | 14 | |
| α-helix | 150-154 | 5 | |
| α-helix | 155-161 | 7 | |
| α-helix | 162-169 | 8 | |
| α-helix | 177-185 | 9 | |
| α-helix | 192-202 | 11 | |
| α-helix | 204-214 | 11 | |
| α-helix | 218-226 | 9 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-248 | 4 | |
| α-helix | 272-288 | 17 | |
| α-helix | 293-331 | 39 | |
| α-helix | 335-365 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-50 | 41 | |
| α-helix | 56-91 | 36 | |
| α-helix | 102-114 | 13 | |
| α-helix | 147-154 | 8 | |
| α-helix | 155-162 | 8 | |
| α-helix | 163-171 | 9 | |
| α-helix | 177-186 | 10 | |
| α-helix | 192-202 | 11 | |
| α-helix | 206-215 | 10 | |
| α-helix | 220-226 | 7 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-248 | 4 | |
| α-helix | 272-288 | 17 | |
| α-helix | 293-331 | 39 | |
| α-helix | 338-365 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-49 | 39 | |
| α-helix | 51-53 | 3 | |
| α-helix | 56-90 | 35 | |
| α-helix | 96-99 | 4 | |
| α-helix | 102-115 | 14 | |
| α-helix | 150-154 | 5 | |
| α-helix | 155-161 | 7 | |
| α-helix | 162-169 | 8 | |
| α-helix | 177-186 | 10 | |
| α-helix | 192-202 | 11 | |
| α-helix | 206-218 | 13 | |
| α-helix | 222-226 | 5 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-248 | 4 | |
| α-helix | 261-269 | 9 | |
| α-helix | 275-288 | 14 | |
| α-helix | 293-331 | 39 | |
| α-helix | 335-365 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-32 | 22 | |
| α-helix | 34-45 | 12 | |
| α-helix | 46-50 | 5 | |
| α-helix | 55-72 | 18 | |
| α-helix | 77-91 | 15 | |
| α-helix | 102-114 | 13 | |
| α-helix | 147-154 | 8 | |
| α-helix | 155-161 | 7 | |
| α-helix | 162-170 | 9 | |
| α-helix | 177-183 | 7 | |
| α-helix | 192-202 | 11 | |
| α-helix | 206-214 | 9 | |
| α-helix | 218-226 | 9 | |
| α-helix | 237-243 | 7 | |
| α-helix | 245-248 | 4 | |
| α-helix | 261-264 | 4 | |
| α-helix | 269-288 | 20 | |
| α-helix | 293-331 | 39 | |
| α-helix | 336-365 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 85-91 | 7 | |
| α-helix | 102-111 | 10 | |
| α-helix | 118-128 | 11 | |
| α-helix | 143-146 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intermediate conductance calcium-activated potassium channel protein 4 | A, B, C, D | protein | 358 | Homo sapiens | O15554 (AlphaFold model) |
| Calmodulin-1 | E, F, G, H | protein | 67 | Homo sapiens | P0DP23 (AlphaFold model) |
>9YDZ_1 Intermediate conductance calcium-activated potassium channel protein 4 (chains A, B, C, D) LGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISIS TFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCV QDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQV RFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITF LTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYT KEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVKLKHRKLREQVN
>9YDZ_2 Calmodulin-1 (chains E, F, G, H) SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEE FVQMMTA
Structural basis for the subtype-selectivity of K Ca 2.2 channel activators. Nam, Y.W., Ramanishka, A., Xu, Y. et al. Nat Commun (2026) 17:531-531. DOI 10.1038/s41467-025-67232-3 · PubMed
Other PDB entries of the same protein (UniProt O15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9YDZ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.