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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_FI1
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S0 => ECO:0000255
ChainResidueDetails
ATRP22-LEU42

site_idSWS_FT_FI2
Number of Residues87
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATRP43-ARG113
AALA171-LYS174
ALEU221-LEU235

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S1 => ECO:0000255
ChainResidueDetails
AVAL114-SER134

site_idSWS_FT_FI4
Number of Residues38
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ASER135-THR149
ASER196-LEU199
AGLU257-GLN270
ATYR294-LEU302

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000255
ChainResidueDetails
ALEU150-ALA170

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S3 => ECO:0000255
ChainResidueDetails
ALEU175-VAL195

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S4 => ECO:0000255
ChainResidueDetails
AASN200-ILE220

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0000255
ChainResidueDetails
AVAL236-VAL256

site_idSWS_FT_FI9
Number of Residues22
DetailsINTRAMEM: Pore-forming; Name=P region => ECO:0000255
ChainResidueDetails
AALA271-VAL293

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000255
ChainResidueDetails
APHE303-ILE323

site_idSWS_FT_FI11
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLU374
AGLN397
AGLU399

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:B7ZC96
ChainResidueDetails
APRO947
AGLU950
AILE953
AGLU955

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q08460
ChainResidueDetails
ALYS698
ALEU905

site_idSWS_FT_FI14
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q08460
ChainResidueDetails
AILE700
ATHR713
AGLY717
ATHR913
AVAL917

site_idSWS_FT_FI15
Number of Residues3
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:20693285, ECO:0000269|PubMed:22399288
ChainResidueDetails
ACYS53
ACYS54
ACYS56

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PDB entries from 2024-09-11

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