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6DMW

Calmodulin-bound full-length rbTRPV5

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0005516molecular_functioncalmodulin binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0035809biological_processregulation of urine volume
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
A0055074biological_processcalcium ion homeostasis
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A0098703biological_processcalcium ion import across plasma membrane
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0005516molecular_functioncalmodulin binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006816biological_processcalcium ion transport
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0035809biological_processregulation of urine volume
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
B0055074biological_processcalcium ion homeostasis
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
B0098655biological_processmonoatomic cation transmembrane transport
B0098703biological_processcalcium ion import across plasma membrane
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0005516molecular_functioncalmodulin binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0035809biological_processregulation of urine volume
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051289biological_processprotein homotetramerization
C0055074biological_processcalcium ion homeostasis
C0055085biological_processtransmembrane transport
C0070588biological_processcalcium ion transmembrane transport
C0098655biological_processmonoatomic cation transmembrane transport
C0098703biological_processcalcium ion import across plasma membrane
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0005516molecular_functioncalmodulin binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006816biological_processcalcium ion transport
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0035809biological_processregulation of urine volume
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051289biological_processprotein homotetramerization
D0055074biological_processcalcium ion homeostasis
D0055085biological_processtransmembrane transport
D0070588biological_processcalcium ion transmembrane transport
D0098655biological_processmonoatomic cation transmembrane transport
D0098703biological_processcalcium ion import across plasma membrane
E0000086biological_processG2/M transition of mitotic cell cycle
E0000922cellular_componentspindle pole
E0001975biological_processresponse to amphetamine
E0002027biological_processregulation of heart rate
E0005246molecular_functioncalcium channel regulator activity
E0005509molecular_functioncalcium ion binding
E0005513biological_processdetection of calcium ion
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005813cellular_componentcentrosome
E0005819cellular_componentspindle
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0005876cellular_componentspindle microtubule
E0008076cellular_componentvoltage-gated potassium channel complex
E0008179molecular_functionadenylate cyclase binding
E0010856molecular_functionadenylate cyclase activator activity
E0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
E0016240biological_processautophagosome membrane docking
E0019855molecular_functioncalcium channel inhibitor activity
E0019901molecular_functionprotein kinase binding
E0019904molecular_functionprotein domain specific binding
E0030017cellular_componentsarcomere
E0030235molecular_functionnitric-oxide synthase regulator activity
E0030426cellular_componentgrowth cone
E0030672cellular_componentsynaptic vesicle membrane
E0031432molecular_functiontitin binding
E0031514cellular_componentmotile cilium
E0031800molecular_functiontype 3 metabotropic glutamate receptor binding
E0031966cellular_componentmitochondrial membrane
E0032465biological_processregulation of cytokinesis
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
E0043548molecular_functionphosphatidylinositol 3-kinase binding
E0044325molecular_functiontransmembrane transporter binding
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0046872molecular_functionmetal ion binding
E0048306molecular_functioncalcium-dependent protein binding
E0050998molecular_functionnitric-oxide synthase binding
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
E0071346biological_processcellular response to type II interferon
E0072542molecular_functionprotein phosphatase activator activity
E0090150biological_processestablishment of protein localization to membrane
E0090151biological_processestablishment of protein localization to mitochondrial membrane
E0097225cellular_componentsperm midpiece
E0098685cellular_componentSchaffer collateral - CA1 synapse
E0098901biological_processregulation of cardiac muscle cell action potential
E0099523cellular_componentpresynaptic cytosol
E0099524cellular_componentpostsynaptic cytosol
E0140056biological_processorganelle localization by membrane tethering
E1900242biological_processregulation of synaptic vesicle endocytosis
E1902494cellular_componentcatalytic complex
E1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
E2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA E 201
ChainResidue
EASP21
EASP23
EASP25
ETHR27
EGLU32

site_idAC2
Number of Residues5
Detailsbinding site for residue CA E 202
ChainResidue
EGLU105
EASP94
EASP96
EASN98
ETYR100

site_idAC3
Number of Residues5
Detailsbinding site for residue CA E 203
ChainResidue
EASP130
EASP132
EASP134
EGLN136
EGLU141

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
EASP21-LEU33
EASP57-PHE69
EASP94-LEU106
EASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
BARG409-THR419
BARG470-ARG492
BMET578-PHE730
CMET1-PRO327
CARG409-THR419
CARG470-ARG492
CMET578-PHE730
DMET1-PRO327
DARG409-THR419
DARG470-ARG492
DMET578-PHE730
EASP21
EASP23
EASP25
ETHR27
EGLU32

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1G4Y, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3B32, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3IFK, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4G27, ECO:0007744|PDB:4G28, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4J9Y, ECO:0007744|PDB:4J9Z, ECO:0007744|PDB:4QNH
ChainResidueDetails
AILE557-MET577
BTYR328-ILE348
BLEU386-PHE408
BILE420-MET442
BGLY449-ALA469
BPHE493-GLN513
BILE557-MET577
CTYR328-ILE348
CLEU386-PHE408
CILE420-MET442
CGLY449-ALA469
CPHE493-GLN513
CILE557-MET577
DTYR328-ILE348
DLEU386-PHE408
DILE420-MET442
DGLY449-ALA469
DPHE493-GLN513
DILE557-MET577
EASP57
EASP59
EASN61
ETHR63
EGLU68

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK4, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG6, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
CARG443-ASN448
DTYR349-ARG385
DARG443-ASN448
EASP94
EASP96
EASN98
ETYR100
EGLU105

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:23109337, ECO:0000269|PubMed:3145979, ECO:0007744|PDB:1NIW, ECO:0007744|PDB:2HQW, ECO:0007744|PDB:2YGG, ECO:0007744|PDB:3BXK, ECO:0007744|PDB:3BXL, ECO:0007744|PDB:3CLN, ECO:0007744|PDB:3EK7, ECO:0007744|PDB:3EK8, ECO:0007744|PDB:3EKH, ECO:0007744|PDB:3EVR, ECO:0007744|PDB:3EVU, ECO:0007744|PDB:3SG2, ECO:0007744|PDB:3SG3, ECO:0007744|PDB:3SG4, ECO:0007744|PDB:3SG5, ECO:0007744|PDB:3SG7, ECO:0007744|PDB:3SJQ, ECO:0007744|PDB:3WLC, ECO:0007744|PDB:3WLD, ECO:0007744|PDB:4EHQ, ECO:0007744|PDB:4I2Y, ECO:0007744|PDB:4RJD
ChainResidueDetails
EGLU141
EASP130
EASP132
EASP134
EGLN136

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:201628, ECO:0000269|Ref.8
ChainResidueDetails
EALA2
BASP542
CASP542
DASP542

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ELYS22
BTHR685
CTHR685
DTHR685

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
ETHR45
BSER689
CSER689
DSER689

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ESER82
BASN358
CASN358
DASN358

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ELYS95

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ETYR100

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ESER102

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ETHR111

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ELYS116

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ETYR139

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
ELYS22

219869

PDB entries from 2024-05-15

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