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2NZ0

Crystal structure of potassium channel Kv4.3 in complex with its regulatory subunit KChIP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005249molecular_functionvoltage-gated potassium channel activity
B0006813biological_processpotassium ion transport
B0008076cellular_componentvoltage-gated potassium channel complex
B0051260biological_processprotein homooligomerization
C0005509molecular_functioncalcium ion binding
D0005249molecular_functionvoltage-gated potassium channel activity
D0006813biological_processpotassium ion transport
D0008076cellular_componentvoltage-gated potassium channel complex
D0051260biological_processprotein homooligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP135
AASN137
ATYR141
AGLU146

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AASN185
AASP187
AILE189
AGLU194

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS131
BCYS132
DCYS110
BHIS104

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 301
ChainResidue
CASP135
CASN137
CTYR141
CASN143
CGLU146

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 302
ChainResidue
CASN185
CASP187
CILE189
CGLU194

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 301
ChainResidue
BCYS110
DHIS104
DCYS131
DCYS132

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DINKDGYINkeEM
ChainResidueDetails
AASP135-MET147
AASP183-PHE195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues26
DetailsRegion: {"description":"Interaction with KCND2","evidences":[{"source":"UniProtKB","id":"Q8R426","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17057713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17187064","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues30
DetailsRegion: {"description":"Interaction with KCNIP1 and KCNIP2","evidences":[{"source":"PubMed","id":"17187064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34997220","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsRegion: {"description":"Interaction with KCNIP1","evidences":[{"source":"PubMed","id":"17187064","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsBinding site: {"description":"in chain B","evidences":[{"source":"PDB","id":"1S1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NZ0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsBinding site: {"description":"in chain D","evidences":[{"source":"PDB","id":"1S1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NZ0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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