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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6E2F

Cryo-EM structure of human TRPV6 in complex with Calmodulin

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
A0035898biological_processparathyroid hormone secretion
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
B0035898biological_processparathyroid hormone secretion
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
C0035898biological_processparathyroid hormone secretion
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
D0035898biological_processparathyroid hormone secretion
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
E0000086biological_processG2/M transition of mitotic cell cycle
E0000922cellular_componentspindle pole
E0002027biological_processregulation of heart rate
E0005246molecular_functioncalcium channel regulator activity
E0005509molecular_functioncalcium ion binding
E0005513biological_processdetection of calcium ion
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005813cellular_componentcentrosome
E0005819cellular_componentspindle
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0005876cellular_componentspindle microtubule
E0005886cellular_componentplasma membrane
E0005929cellular_componentcilium
E0007186biological_processG protein-coupled receptor signaling pathway
E0007259biological_processcell surface receptor signaling pathway via JAK-STAT
E0008076cellular_componentvoltage-gated potassium channel complex
E0010856molecular_functionadenylate cyclase activator activity
E0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
E0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
E0016020cellular_componentmembrane
E0016240biological_processautophagosome membrane docking
E0019855molecular_functioncalcium channel inhibitor activity
E0019901molecular_functionprotein kinase binding
E0021762biological_processsubstantia nigra development
E0030017cellular_componentsarcomere
E0030672cellular_componentsynaptic vesicle membrane
E0031432molecular_functiontitin binding
E0031514cellular_componentmotile cilium
E0031982cellular_componentvesicle
E0032465biological_processregulation of cytokinesis
E0032991cellular_componentprotein-containing complex
E0034704cellular_componentcalcium channel complex
E0035458biological_processcellular response to interferon-beta
E0042995cellular_componentcell projection
E0043209cellular_componentmyelin sheath
E0043539molecular_functionprotein serine/threonine kinase activator activity
E0044305cellular_componentcalyx of Held
E0044325molecular_functiontransmembrane transporter binding
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0046872molecular_functionmetal ion binding
E0048306molecular_functioncalcium-dependent protein binding
E0050848biological_processregulation of calcium-mediated signaling
E0051592biological_processresponse to calcium ion
E0055117biological_processregulation of cardiac muscle contraction
E0060291biological_processlong-term synaptic potentiation
E0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
E0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
E0071346biological_processcellular response to type II interferon
E0072542molecular_functionprotein phosphatase activator activity
E0097225cellular_componentsperm midpiece
E0097720biological_processcalcineurin-mediated signaling
E0098901biological_processregulation of cardiac muscle cell action potential
E0099523cellular_componentpresynaptic cytosol
E0140056biological_processorganelle localization by membrane tethering
E0140238biological_processpresynaptic endocytosis
E0141110molecular_functiontransporter inhibitor activity
E1901842biological_processnegative regulation of high voltage-gated calcium channel activity
E1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
E1902494cellular_componentcatalytic complex
E1905913biological_processnegative regulation of calcium ion export across plasma membrane
E1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CA A 901
ChainResidue
AASP542
ACA902
BASP542
DASP542
site_idAC2
Number of Residues1
Detailsbinding site for residue CA A 902
ChainResidue
ACA901
site_idAC3
Number of Residues4
Detailsbinding site for residue CA E 401
ChainResidue
EASP20
ETHR26
EILE27
EGLU31
site_idAC4
Number of Residues6
Detailsbinding site for residue CA E 402
ChainResidue
EASP56
EASP58
EASN60
ETHR62
EASP64
EGLU67
site_idAC5
Number of Residues5
Detailsbinding site for residue CA E 403
ChainResidue
EASP93
EASP95
EASN97
ETYR99
EGLU104
site_idAC6
Number of Residues6
Detailsbinding site for residue CA E 404
ChainResidue
EASP129
EASP131
EASP133
EGLN135
EASN137
EGLU140
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
EASP20-LEU32
EASP56-PHE68
EASP93-LEU105
EASP129-PHE141
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues488
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 Residues132
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
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKC/PRKCA","evidences":[{"source":"PubMed","id":"11248124","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues32
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues72
DetailsRegion: {"description":"Necessary and sufficient for interaction with PCP4","evidences":[{"source":"PubMed","id":"27876793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues5
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_FI25
Number of Residues5
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_FI26
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7093203","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
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_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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