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7UKD

Human Kv4.2-KChIP2 channel complex in an inactivated state, class 2, transmembrane region

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 Residues820
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AMET1-THR182
DMET1-THR182
DALA251-VAL261
DSER307-ALA321
AALA251-VAL261
ASER307-ALA321
BMET1-THR182
BALA251-VAL261
BSER307-ALA321
CMET1-THR182
CALA251-VAL261
CSER307-ALA321

site_idSWS_FT_FI2
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S1 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AMET183-VAL204
BMET183-VAL204
CMET183-VAL204
DMET183-VAL204

site_idSWS_FT_FI3
Number of Residues192
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AGLU205-ALA228
CTHR280-SER286
CTYR344-ILE357
CPRO378-LYS384
DGLU205-ALA228
DTHR280-SER286
DTYR344-ILE357
DPRO378-LYS384
ATHR280-SER286
ATYR344-ILE357
APRO378-LYS384
BGLU205-ALA228
BTHR280-SER286
BTYR344-ILE357
BPRO378-LYS384
CGLU205-ALA228

site_idSWS_FT_FI4
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
APHE229-ALA250
BPHE229-ALA250
CPHE229-ALA250
DPHE229-ALA250

site_idSWS_FT_FI5
Number of Residues68
DetailsTRANSMEM: Helical; Name=Segment S3 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AMET262-MET279
BMET262-MET279
CMET262-MET279
DMET262-MET279

site_idSWS_FT_FI6
Number of Residues76
DetailsTRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AGLY287-HIS306
BGLY287-HIS306
CGLY287-HIS306
DGLY287-HIS306

site_idSWS_FT_FI7
Number of Residues84
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
ASER322-PHE343
BSER322-PHE343
CSER322-PHE343
DSER322-PHE343

site_idSWS_FT_FI8
Number of Residues44
DetailsINTRAMEM: Helical; Name=Pore helix => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
APRO358-THR369
BPRO358-THR369
CPRO358-THR369
DPRO358-THR369

site_idSWS_FT_FI9
Number of Residues28
DetailsINTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
ATHR370-VAL377
BTHR370-VAL377
CTHR370-VAL377
DTHR370-VAL377

site_idSWS_FT_FI10
Number of Residues112
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
AILE385-TYR413
BILE385-TYR413
CILE385-TYR413
DILE385-TYR413

site_idSWS_FT_FI11
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q63881
ChainResidueDetails
AHIS105
DHIS105
DCYS132
DCYS133
ACYS132
ACYS133
BHIS105
BCYS132
BCYS133
CHIS105
CCYS132
CCYS133

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q63881
ChainResidueDetails
ATHR38
BTHR38
CTHR38
DTHR38

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q63881
ChainResidueDetails
ASER438
BSER438
CSER438
DSER438

222036

PDB entries from 2024-07-03

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