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7E83

CryoEM structure of the human Kv4.2-KChIP1 complex, intracellular 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
B0005509molecular_functioncalcium ion binding
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
E0005509molecular_functioncalcium ion binding
F0005509molecular_functioncalcium ion binding
G0005216molecular_functionmonoatomic ion channel activity
G0005249molecular_functionvoltage-gated potassium channel activity
G0006811biological_processmonoatomic ion transport
G0006813biological_processpotassium ion transport
G0008076cellular_componentvoltage-gated potassium channel complex
G0016020cellular_componentmembrane
G0051260biological_processprotein homooligomerization
G0055085biological_processtransmembrane transport
H0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DINKDGYINkeEM
ChainResidueDetails
EASP135-MET147
EASP183-PHE195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:17057713, ECO:0000269|PubMed:17187064
ChainResidueDetails
EASP135
BASP135
BASN137
BASP139
BTYR141
BGLU146
BASP183
BASN185
BASP187
BGLU194
FASP135
EASN137
FASN137
FASP139
FTYR141
FGLU146
FASP183
FASN185
FASP187
FGLU194
HASP135
HASN137
EASP139
HASP139
HTYR141
HGLU146
HASP183
HASN185
HASP187
HGLU194
ETYR141
EGLU146
EASP183
EASN185
EASP187
EGLU194

site_idSWS_FT_FI2
Number of Residues148
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:34552243
ChainResidueDetails
CVAL207-ALA226
DASN282-GLY287
DGLU346-ILE357
DPRO378-THR380
GVAL207-ALA226
GASN282-GLY287
GGLU346-ILE357
GPRO378-THR380
CASN282-GLY287
CGLU346-ILE357
CPRO378-THR380
AVAL207-ALA226
AASN282-GLY287
AGLU346-ILE357
APRO378-THR380
DVAL207-ALA226

site_idSWS_FT_FI3
Number of Residues88
DetailsTRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CVAL227-ALA249
AVAL227-ALA249
DVAL227-ALA249
GVAL227-ALA249

site_idSWS_FT_FI4
Number of Residues76
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:34552243
ChainResidueDetails
CALA250-ARG256
CGLN308-ALA321
AALA250-ARG256
AGLN308-ALA321
DALA250-ARG256
DGLN308-ALA321
GALA250-ARG256
GGLN308-ALA321

site_idSWS_FT_FI5
Number of Residues96
DetailsTRANSMEM: Helical; Name=Segment S3 => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CPHE257-ASP281
APHE257-ASP281
DPHE257-ASP281
GPHE257-ASP281

site_idSWS_FT_FI6
Number of Residues76
DetailsTRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CALA288-SER307
AALA288-SER307
DALA288-SER307
GALA288-SER307

site_idSWS_FT_FI7
Number of Residues92
DetailsTRANSMEM: Helical; Name=Segment S5 => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CSER322-ALA345
ASER322-ALA345
DSER322-ALA345
GSER322-ALA345

site_idSWS_FT_FI8
Number of Residues44
DetailsINTRAMEM: Helical; Name=Pore helix => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
CPRO358-THR369
APRO358-THR369
DPRO358-THR369
GPRO358-THR369

site_idSWS_FT_FI9
Number of Residues28
DetailsINTRAMEM: INTRAMEM => ECO:0000250|UniProtKB:P63142
ChainResidueDetails
CTHR370-VAL377
ATHR370-VAL377
DTHR370-VAL377
GTHR370-VAL377

site_idSWS_FT_FI10
Number of Residues88
DetailsTRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CILE381-PRO403
AILE381-PRO403
DILE381-PRO403
GILE381-PRO403

site_idSWS_FT_FI11
Number of Residues12
DetailsBINDING: in chain A => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CHIS105
GHIS105
GCYS132
GCYS133
CCYS132
CCYS133
AHIS105
ACYS132
ACYS133
DHIS105
DCYS132
DCYS133

site_idSWS_FT_FI12
Number of Residues4
DetailsBINDING: in chain B => ECO:0000269|PubMed:34552243, ECO:0007744|PDB:7F0J
ChainResidueDetails
CCYS111
ACYS111
DCYS111
GCYS111

site_idSWS_FT_FI13
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:35597238, ECO:0007744|PDB:7UK5, ECO:0007744|PDB:7UKD, ECO:0007744|PDB:7UKE, ECO:0007744|PDB:7UKF
ChainResidueDetails
CTHR370
CTYR373
ATHR370
ATYR373
DTHR370
DTYR373
GTHR370
GTYR373

site_idSWS_FT_FI14
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:35597238, ECO:0007744|PDB:7UKC, ECO:0007744|PDB:7UKG
ChainResidueDetails
CLEU371
ALEU371
DLEU371
GLEU371

site_idSWS_FT_FI15
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:35597238, ECO:0007744|PDB:7UK5, ECO:0007744|PDB:7UKC, ECO:0007744|PDB:7UKD, ECO:0007744|PDB:7UKE, ECO:0007744|PDB:7UKF, ECO:0007744|PDB:7UKG
ChainResidueDetails
CGLY372
AGLY372
DGLY372
GGLY372

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q63881
ChainResidueDetails
CTHR38
ATHR38
DTHR38
GTHR38

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q63881
ChainResidueDetails
CSER438
ASER438
DSER438
GSER438

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PDB entries from 2024-07-31

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