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7YO3

Cryo-EM structure of human Slo1-LRRC26 complex with C4 symmetry

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. VITNPPY
ChainResidueDetails
AVAL1033-TYR1039

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues142
DetailsDomain: {"description":"RCK N-terminal 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00543","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S0","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues38
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues17
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues22
DetailsIntramembrane: {"description":"Pore-forming; Name=P region","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsRegion: {"description":"Segment S7"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsRegion: {"description":"Segment S9"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues20
DetailsRegion: {"description":"Segment S10"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues3
DetailsMotif: {"description":"Selectivity for potassium"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues22
DetailsMotif: {"description":"Calcium bowl","evidences":[{"source":"UniProtKB","id":"B7ZC96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"B7ZC96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues21
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues21
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues21
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues23
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues22
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues54
DetailsDomain: {"description":"LRRCT"}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22547800","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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