Ca2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in nanodisc. Determined by electron microscopy at 2.57 Å resolution. Released 5 Mar 2025.
Explore 9CZM in 3D Show helices and sheets RCSB PDB PDBe
9CZM contains 209 α-helices and 156 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 | 22-53 | 32 | |
| α-helix | 93-105 | 13 | |
| α-helix | 110-133 | 24 | |
| β-strand | 139-141 | 3 | 7 |
| α-helix | 148-170 | 23 | |
| α-helix | 174-178 | 5 | |
| α-helix | 181-187 | 7 | |
| α-helix | 191-199 | 9 | |
| β-strand | 201-203 | 3 | 7 |
| α-helix | 206-216 | 11 | |
| α-helix | 217-223 | 7 | |
| α-helix | 230-258 | 29 | |
| α-helix | 274-285 | 12 | |
| α-helix | 298-324 | 27 | |
| β-strand | 339 | 1 | 8 |
| β-strand | 342 | 1 | 8 |
| β-strand | 344-349 | 6 | 9 |
| α-helix | 353-363 | 11 | |
| β-strand | 374-379 | 6 | 9 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-392 | 8 | |
| β-strand | 398-402 | 5 | 9 |
| α-helix | 408-413 | 6 | |
| α-helix | 416-418 | 3 | |
| β-strand | 421-425 | 5 | 9 |
| α-helix | 433-450 | 18 | |
| β-strand | 456-460 | 5 | 9 |
| α-helix | 463-469 | 7 | |
| α-helix | 477-479 | 3 | |
| β-strand | 482-485 | 4 | 9 |
| α-helix | 486-499 | 14 | |
| α-helix | 503-511 | 9 | |
| α-helix | 524-532 | 9 | |
| β-strand | 535-540 | 6 | 10 |
| α-helix | 550-559 | 10 | |
| β-strand | 564 | 1 | 10 |
| β-strand | 568 | 1 | 11 |
| β-strand | 581 | 1 | 11 |
| β-strand | 594-599 | 6 | 10 |
| α-helix | 602-605 | 4 | |
| α-helix | 606-608 | 3 | |
| β-strand | 686-687 | 2 | 12 |
| β-strand | 692 | 1 | 13 |
| β-strand | 693 | 1 | 12 |
| α-helix | 700-703 | 4 | |
| β-strand | 704 | 1 | 14 |
| α-helix | 707-712 | 6 | |
| β-strand | 718-724 | 7 | 14 |
| α-helix | 730-731 | 2 | |
| α-helix | 735-738 | 4 | |
| α-helix | 740-742 | 3 | |
| β-strand | 743 | 1 | 13 |
| β-strand | 754-758 | 5 | 14 |
| α-helix | 760-770 | 11 | |
| β-strand | 776-780 | 5 | 14 |
| α-helix | 786-791 | 6 | |
| α-helix | 794-796 | 3 | |
| β-strand | 797-804 | 8 | 14 |
| α-helix | 818-829 | 12 | |
| β-strand | 878-881 | 4 | 14 |
| α-helix | 885-890 | 6 | |
| α-helix | 903-905 | 3 | |
| α-helix | 907-910 | 4 | |
| β-strand | 914-915 | 2 | 14 |
| α-helix | 917-921 | 5 | |
| α-helix | 922-929 | 8 | |
| α-helix | 933-942 | 10 | |
| α-helix | 947-956 | 10 | |
| α-helix | 959-960 | 2 | |
| β-strand | 961-962 | 2 | 12 |
| α-helix | 966-970 | 5 | |
| β-strand | 976-981 | 6 | 15 |
| α-helix | 988-993 | 6 | |
| β-strand | 995 | 1 | 16 |
| β-strand | 1011-1017 | 7 | 15 |
| β-strand | 1031-1035 | 5 | 15 |
| β-strand | 1042 | 1 | 16 |
| β-strand | 1047-1053 | 7 | 15 |
| α-helix | 1054-1055 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-77 | 37 | |
| β-strand | 80-84 | 5 | 1 |
| β-strand | 85-99 | 15 | 2 |
| β-strand | 109-120 | 12 | 2 |
| β-strand | 128-130 | 3 | 2 |
| α-helix | 134-139 | 6 | |
| α-helix | 153-169 | 17 | |
| α-helix | 173 | 1 | |
| α-helix | 175 | 1 | |
| β-strand | 176-181 | 6 | 1 |
| β-strand | 185-190 | 6 | 1 |
| α-helix | 197-234 | 38 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| α-helix | 41-77 | 37 | |
| β-strand | 80-84 | 5 | 47 |
| β-strand | 85-99 | 15 | 48 |
| β-strand | 109-120 | 12 | 48 |
| β-strand | 128-130 | 3 | 48 |
| α-helix | 134-139 | 6 | |
| α-helix | 153-169 | 17 | |
| α-helix | 173 | 1 | |
| α-helix | 175 | 1 | |
| β-strand | 176-181 | 6 | 47 |
| β-strand | 185-190 | 6 | 47 |
| α-helix | 197-234 | 38 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Large-conductance Ca2+-activated K+ channel beta2 subunit,Calcium-activated potassium channel… | E, F, G, H | protein | 239 | Homo sapiens | B5BNX0 (AlphaFold model), Q86W47 (AlphaFold model) |
| Isoform 5 of Calcium-activated potassium channel subunit alpha-1 | A, B, C, D | protein | 1056 | Homo sapiens | Q12791 (AlphaFold model) |
>9CZM_1 Large-conductance Ca2+-activated K+ channel beta2 subunit,Calcium-activated potassium channel subunit beta-4 (chains E, F, G, H) FIWTSGRTSSSYRHDEKRNIYQKIRDHDLLDKRKTVTALKAGEDKSIRLGLFLIISGVVS LFIFGFCWLSPALQDLQATEANCTVLSVQQIGEVFECTFTCGADCRGTSQYPCVQVYVNN SESNSRALLHSDEHQLLTNPKCSYIPPCKRENQKNLESVMNWQQYWKDEIGSQPFTCYFN QHQRPDDVLLHRTHDEIVLLHCFLWPLVTFVVGVLIVVLTICAKSLAVKAEAMKKRKFS
>9CZM_2 Isoform 5 of Calcium-activated potassium channel subunit alpha-1 (chains A, B, C, D) MDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKT KEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVF ALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLE VNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLS IFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLG RLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFL KDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESAD ACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEG DDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEY LSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIAS DAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNTSP KLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVV VCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILP GTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQ ANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPD TELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALR GGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDA HLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFD
| ID | Name | Formula | Copies |
|---|---|---|---|
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 32 |
| MG | Magnesium ion | Mg | 4 |
| CA | Calcium ion | Ca | 8 |
| CLR | Cholesterol | C27 H46 O | 8 |
Water and common crystallization additives (K) are not listed.
Ball-and-chain inactivation of a human large conductance calcium-activated potassium channel. Agarwal, S., Kim, E.D., Lee, S. et al. Nat Commun (2025) 16:1769-1769. DOI 10.1038/s41467-025-56844-4 · PubMed
Other PDB entries of the same protein (UniProt B5BNX0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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