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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6BOA

Cryo-EM structure of human TRPV6-R470E in amphipols

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0016020cellular_componentmembrane
A0017158biological_processregulation of calcium ion-dependent exocytosis
A0034220biological_processmonoatomic ion transmembrane transport
A0034704cellular_componentcalcium channel complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051592biological_processresponse to calcium ion
A0055074biological_processcalcium ion homeostasis
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0098703biological_processcalcium ion import across plasma membrane
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006816biological_processcalcium ion transport
B0016020cellular_componentmembrane
B0017158biological_processregulation of calcium ion-dependent exocytosis
B0034220biological_processmonoatomic ion transmembrane transport
B0034704cellular_componentcalcium channel complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051592biological_processresponse to calcium ion
B0055074biological_processcalcium ion homeostasis
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
B0098703biological_processcalcium ion import across plasma membrane
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0005515molecular_functionprotein binding
C0005516molecular_functioncalmodulin binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0016020cellular_componentmembrane
C0017158biological_processregulation of calcium ion-dependent exocytosis
C0034220biological_processmonoatomic ion transmembrane transport
C0034704cellular_componentcalcium channel complex
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051592biological_processresponse to calcium ion
C0055074biological_processcalcium ion homeostasis
C0055085biological_processtransmembrane transport
C0070588biological_processcalcium ion transmembrane transport
C0098703biological_processcalcium ion import across plasma membrane
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0005515molecular_functionprotein binding
D0005516molecular_functioncalmodulin binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006816biological_processcalcium ion transport
D0016020cellular_componentmembrane
D0017158biological_processregulation of calcium ion-dependent exocytosis
D0034220biological_processmonoatomic ion transmembrane transport
D0034704cellular_componentcalcium channel complex
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051592biological_processresponse to calcium ion
D0055074biological_processcalcium ion homeostasis
D0055085biological_processtransmembrane transport
D0070588biological_processcalcium ion transmembrane transport
D0098703biological_processcalcium ion import across plasma membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues400
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues252
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues76
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues76
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues120
DetailsRepeat: {"description":"ANK 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues116
DetailsRepeat: {"description":"ANK 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues116
DetailsRepeat: {"description":"ANK 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues116
DetailsRepeat: {"description":"ANK 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues168
DetailsRepeat: {"description":"ANK 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues116
DetailsRepeat: {"description":"ANK 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsRegion: {"description":"Interaction with calmodulin","evidences":[{"source":"UniProtKB","id":"Q91WD2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues16
DetailsRegion: {"description":"Interaction with S100A10","evidences":[{"source":"UniProtKB","id":"Q91WD2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues16
DetailsMotif: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29258289","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"Q9R186","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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