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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6EBM

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

Functional Information from GO Data
ChainGOidnamespacecontents
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
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
F0005216molecular_functionmonoatomic ion channel activity
F0005249molecular_functionvoltage-gated potassium channel activity
F0006811biological_processmonoatomic ion transport
F0006813biological_processpotassium ion transport
F0008076cellular_componentvoltage-gated potassium channel complex
F0016020cellular_componentmembrane
F0051260biological_processprotein homooligomerization
F0055085biological_processtransmembrane transport
H0005216molecular_functionmonoatomic ion channel activity
H0005249molecular_functionvoltage-gated potassium channel activity
H0006811biological_processmonoatomic ion transport
H0006813biological_processpotassium ion transport
H0008076cellular_componentvoltage-gated potassium channel complex
H0016020cellular_componentmembrane
H0051260biological_processprotein homooligomerization
H0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues152
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18004376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360102","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20534430","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12151401","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"source":"PubMed","id":"18004376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360102","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20534430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues104
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18004376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360102","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20534430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"source":"PubMed","id":"18004376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20360102","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20534430","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues44
DetailsIntramembrane: {"description":"Helical; Name=Pore helix","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues28
DetailsIntramembrane: {"evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues116
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues112
DetailsTransmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues52
DetailsRegion: {"description":"S4-S5 linker","evidences":[{"source":"PubMed","id":"16002579","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues20
DetailsMotif: {"description":"Selectivity filter","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsSite: {"description":"Important for normal, slow channel gating","evidences":[{"source":"PubMed","id":"17766348","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsSite: {"description":"Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin","evidences":[{"source":"PubMed","id":"25514171","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16770729","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues72
DetailsTransmembrane: {"description":"Helical; Name=Segment S3","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Voltage-sensor; Name=Segment S4","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"source":"UniProtKB","id":"P63142","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-10-15

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