Cryo-EM structure of the human SK4/calmodulin channel complex. Determined by electron microscopy at 3.4 Å resolution. Released 2 May 2018.
Explore 6CNM in 3D Show helices and sheets RCSB PDB PDBe
6CNM contains 76 α-helices and 8 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 | 12-50 | 39 | |
| α-helix | 57-91 | 35 | |
| α-helix | 96-99 | 4 | |
| α-helix | 104-114 | 11 | |
| α-helix | 149-154 | 6 | |
| α-helix | 157-161 | 5 | |
| α-helix | 162-170 | 9 | |
| α-helix | 177-186 | 10 | |
| α-helix | 192-202 | 11 | |
| α-helix | 204-226 | 23 | |
| α-helix | 237-248 | 12 | |
| α-helix | 261-287 | 27 | |
| α-helix | 293-330 | 38 | |
| α-helix | 338-368 | 31 | |
| α-helix | 370-384 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-50 | 39 | |
| α-helix | 57-91 | 35 | |
| α-helix | 96-99 | 4 | |
| α-helix | 104-114 | 11 | |
| α-helix | 149-154 | 6 | |
| α-helix | 157-161 | 5 | |
| α-helix | 162-170 | 9 | |
| α-helix | 177-186 | 10 | |
| α-helix | 192-202 | 11 | |
| α-helix | 204-226 | 23 | |
| α-helix | 237-248 | 12 | |
| α-helix | 261-287 | 27 | |
| α-helix | 293-330 | 38 | |
| α-helix | 338-368 | 31 | |
| α-helix | 370-383 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 82-89 | 8 | |
| β-strand | 99-101 | 3 | 1 |
| α-helix | 102-111 | 10 | |
| α-helix | 118-128 | 11 | |
| β-strand | 135-137 | 3 | 1 |
| α-helix | 138-145 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Intermediate conductance calcium-activated potassium channel protein 4 | A, B, C, D | protein | 427 | Homo sapiens | O15554 (AlphaFold model) |
| Calmodulin-1 | E, F, G, H | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
>6CNM_1 Intermediate conductance calcium-activated potassium channel protein 4 (chains A, B, C, D) MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFL VKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPA PVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYR SIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDT LWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHN FMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRK LREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLP EPSQQSK
>6CNM_2 Calmodulin-1 (chains E, F, G, H) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
| ID | Name | Formula | Copies |
|---|---|---|---|
| LMT | Dodecyl-beta-D-maltoside | C24 H46 O11 | 8 |
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 4 |
Water and common crystallization additives (K) are not listed.
Activation mechanism of a human SK-calmodulin channel complex elucidated by cryo-EM structures. Lee, C.H., MacKinnon, R. Science (2018) 360:508-513. DOI 10.1126/science.aas9466 · PubMed
Other PDB entries of the same protein (UniProt O15554 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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