8GHF: HSlo1 in plasma membrane vesicles

cryo-EM structure of hSlo1 in plasma membrane vesicles. Determined by electron microscopy at 2.7 Å resolution. Released 10 May 2023.

Method

Electron microscopy

Resolution

2.7 Å

Organism

Homo sapiens

Chains

4

Atoms

31,920

Mol. weight

566.44 kDa

Ligands

CLR, POV, CA, MG

Released

10 May 2023

Explore 8GHF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GHF contains 188 α-helices and 136 β-strands across 4 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: 47 helices, 34 β-strands

Molecules and chains

>8GHF_1 Calcium-activated potassium channel subunit alpha-1 (chains A, B, C, D)
MAPSRLEEELRRRLTEPDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWR
TLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVM
ISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYF
GLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFL
NILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVT
MSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKH
IVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGS
VLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYH
NKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTW
QKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPG
NHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPK
KKQRNGGMRNSPNTSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVI
LTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLK
REWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILAS
LNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVN
DTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGG
ATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKAL
KTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDXXXXXXXX
XXXXXXXXXX

Ligands and cofactors

Water and common crystallization additives (NA) are not listed.

Primary citation

Membrane protein isolation and structure determination in cell-derived membrane vesicles. Tao, X., Zhao, C., MacKinnon, R. Proc Natl Acad Sci U S A (2023) 120:e2302325120-e2302325120. DOI 10.1073/pnas.2302325120 · PubMed

Related structures

Other PDB entries of the same protein (UniProt Q12791 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 6V5A 2.0 Å, Crystal structure of the human BK channel gating ring L390P mutant
• 8V60 2.43 Å, F315A mutant of human Slo1 in presence of EDTA - resting VSD
• 11DA 2.57 Å, Human Slo1-PenitremA complex under divalent chelated condition - full model
• 9CZM 2.57 Å, Ca2+ bound open-inactivated hSlo1 + beta2N-beta4 channel in nanodisc.
• 11DC 2.58 Å, Human Slo1-PenitremA complex under divalent chelated condition - gating-ring masked out
• 11CZ 2.6 Å, Human Slo1-paxilline complex under divalent chelated condition - full model
• 8V64 2.6 Å, RCK1-RCK2 double mutant of human Slo1 in presence of EDTA - resting VSD
• 11DB 2.71 Å, Human Slo1-Paxilline complex under divalent chelated condition - gating-ring masked
• 8V63 2.72 Å, R207A mutant of human Slo1 in presence of EDTA - activated VSD
• 9JO3 2.8 Å, Cryo-EM structure of human BKca channel-compound 10b complex
• 8VAZ 2.82 Å, Structure of human Slo1 and human LRRC26 in EDTA - LRRD masked
• 9CZO 2.87 Å, Ca2+ bound intermediate state of hSlo1 + beta2N-beta4 channel in nanodisc.

Browse structure collections

About this viewer

MolViewer shows 8GHF 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.