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7SIP

Structure of shaker-IR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005249molecular_functionvoltage-gated potassium channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0008076cellular_componentvoltage-gated potassium channel complex
A0016020cellular_componentmembrane
A0051260biological_processprotein homooligomerization
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005249molecular_functionvoltage-gated potassium channel activity
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0008076cellular_componentvoltage-gated potassium channel complex
B0016020cellular_componentmembrane
B0051260biological_processprotein homooligomerization
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005249molecular_functionvoltage-gated potassium channel activity
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0008076cellular_componentvoltage-gated potassium channel complex
C0016020cellular_componentmembrane
C0051260biological_processprotein homooligomerization
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005249molecular_functionvoltage-gated potassium channel activity
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0008076cellular_componentvoltage-gated potassium channel complex
D0016020cellular_componentmembrane
D0051260biological_processprotein homooligomerization
D0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S1 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AALA225-LEU246
BALA225-LEU246
CALA225-LEU246
DALA225-LEU246

site_idSWS_FT_FI2
Number of Residues296
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AGLU247-PRO278
CGLU333-SER357
CPHE416-ILE429
CPRO450-LYS456
DGLU247-PRO278
DGLU333-SER357
DPHE416-ILE429
DPRO450-LYS456
AGLU333-SER357
APHE416-ILE429
APRO450-LYS456
BGLU247-PRO278
BGLU333-SER357
BPHE416-ILE429
BPRO450-LYS456
CGLU247-PRO278

site_idSWS_FT_FI3
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
APHE279-ALA300
BPHE279-ALA300
CPHE279-ALA300
DPHE279-ALA300

site_idSWS_FT_FI4
Number of Residues772
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
ACYS301-VAL311
DCYS301-VAL311
DSER379-MET393
DHIS486-ASP655
ASER379-MET393
AHIS486-ASP655
BCYS301-VAL311
BSER379-MET393
BHIS486-ASP655
CCYS301-VAL311
CSER379-MET393
CHIS486-ASP655

site_idSWS_FT_FI5
Number of Residues80
DetailsTRANSMEM: Helical; Name=Segment S3 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AMET312-ALA332
BMET312-ALA332
CMET312-ALA332
DMET312-ALA332

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
ALEU358-HIS378
BLEU358-HIS378
CLEU358-HIS378
DLEU358-HIS378

site_idSWS_FT_FI7
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AARG394-TYR415
BARG394-TYR415
CARG394-TYR415
DARG394-TYR415

site_idSWS_FT_FI8
Number of Residues44
DetailsINTRAMEM: Helical; Name=Pore helix => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
APRO430-THR441
BPRO430-THR441
CPRO430-THR441
DPRO430-THR441

site_idSWS_FT_FI9
Number of Residues28
DetailsINTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
ATHR442-THR449
BTHR442-THR449
CTHR442-THR449
DTHR442-THR449

site_idSWS_FT_FI10
Number of Residues112
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AILE457-TYR485
BILE457-TYR485
CILE457-TYR485
DILE457-TYR485

site_idSWS_FT_FI11
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17893096
ChainResidueDetails
AASN259
AASN263
BASN259
BASN263
CASN259
CASN263
DASN259
DASN263

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PDB entries from 2025-06-18

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