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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
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
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
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
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
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
E0007186biological_processG protein-coupled receptor signaling pathway
E0008076cellular_componentvoltage-gated potassium channel complex
E0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
E0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
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
E0031432molecular_functiontitin binding
E0031514cellular_componentmotile cilium
E0031954biological_processpositive regulation of protein autophosphorylation
E0031982cellular_componentvesicle
E0032465biological_processregulation of cytokinesis
E0032516biological_processpositive regulation of phosphoprotein phosphatase activity
E0032991cellular_componentprotein-containing complex
E0034704cellular_componentcalcium channel complex
E0035307biological_processpositive regulation of protein dephosphorylation
E0035458biological_processcellular response to interferon-beta
E0043209cellular_componentmyelin sheath
E0043539molecular_functionprotein serine/threonine kinase activator activity
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
E0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
E0051592biological_processresponse to calcium ion
E0055117biological_processregulation of cardiac muscle contraction
E0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
E0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
E0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
E0071346biological_processcellular response to type II interferon
E0071902biological_processpositive regulation of protein serine/threonine kinase activity
E0072542molecular_functionprotein phosphatase activator activity
E0097225cellular_componentsperm midpiece
E0098901biological_processregulation of cardiac muscle cell action potential
E0140056biological_processorganelle localization by membrane tethering
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 Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
ChainResidueDetails
EASP20
EGLU67
BLEU490-PHE512
BILE557-MET577
CTYR328-ILE348
CLEU386-PHE408
CPRO424-ARG443
CGLU450-ALA469
CLEU490-PHE512
CILE557-MET577
DTYR328-ILE348
EASP22
DLEU386-PHE408
DPRO424-ARG443
DGLU450-ALA469
DLEU490-PHE512
DILE557-MET577
EASP24
ETHR26
EGLU31
EASP56
EASP58
EASN60
ETHR62

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
EASP93
EGLU140
CGLN513-ASP525
CASN546-SER556
DTYR349-ARG385
DLEU444-GLY449
DGLN513-ASP525
DASN546-SER556
EASP95
EASN97
ETYR99
EGLU104
EASP129
EASP131
EASP133
EGLN135

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
EALA1
DARG409-GLY423
DARG470-ASP489
DMET578-ILE725
AARG470-ASP489
AMET578-ILE725
BARG409-GLY423
BARG470-ASP489
BMET578-ILE725
CARG409-GLY423
CARG470-ASP489
CMET578-ILE725

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ELYS21
BTYR526-ALA545
CTYR526-ALA545
DTYR526-ALA545

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
ETHR44
BASP542
CASP542
DASP542

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ESER81
BTYR161
CTYR161
DTYR161

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ELYS94
BTHR702
CTHR702
DTHR702

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
ETYR99
BASN358
CASN358
DASN358

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ESER101

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ETHR110

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
ELYS115

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ETYR138

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ELYS21

223532

PDB entries from 2024-08-07

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