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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9YDZ

Cryo EM structure of KCa3.1_R355K_II/calmodulin channel in complex with rimtuzalcap

Functional Information from GO Data
ChainGOidnamespacecontents
A0005516molecular_functioncalmodulin binding
A0006813biological_processpotassium ion transport
A0015269molecular_functioncalcium-activated potassium channel activity
A0016020cellular_componentmembrane
A0016286molecular_functionsmall conductance calcium-activated potassium channel activity
B0005516molecular_functioncalmodulin binding
B0006813biological_processpotassium ion transport
B0015269molecular_functioncalcium-activated potassium channel activity
B0016020cellular_componentmembrane
B0016286molecular_functionsmall conductance calcium-activated potassium channel activity
C0005516molecular_functioncalmodulin binding
C0006813biological_processpotassium ion transport
C0015269molecular_functioncalcium-activated potassium channel activity
C0016020cellular_componentmembrane
C0016286molecular_functionsmall conductance calcium-activated potassium channel activity
D0005516molecular_functioncalmodulin binding
D0006813biological_processpotassium ion transport
D0015269molecular_functioncalcium-activated potassium channel activity
D0016020cellular_componentmembrane
D0016286molecular_functionsmall conductance calcium-activated potassium channel activity
E0005509molecular_functioncalcium ion binding
F0005509molecular_functioncalcium ion binding
G0005509molecular_functioncalcium ion binding
H0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL
ChainResidueDetails
EASP93-LEU105
EASP129-PHE141
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues80
DetailsIntramembrane: {"description":"Pore-forming; Name=Segment H5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=Segment S6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues244
DetailsRegion: {"description":"Calmodulin-binding"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"17157250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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