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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6O20

Cryo-EM structure of TRPV5 with calmodulin bound

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
A0034220biological_processmonoatomic ion transmembrane transport
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
A0097553biological_processcalcium ion transmembrane import into cytosol
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
B0034220biological_processmonoatomic ion transmembrane transport
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
B0097553biological_processcalcium ion transmembrane import into cytosol
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
C0034220biological_processmonoatomic ion transmembrane transport
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
C0097553biological_processcalcium ion transmembrane import into cytosol
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
D0034220biological_processmonoatomic ion transmembrane transport
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
D0097553biological_processcalcium ion transmembrane import into cytosol
D0098703biological_processcalcium ion import across plasma membrane
E0005216molecular_functionmonoatomic ion channel activity
E0005262molecular_functioncalcium channel activity
E0005516molecular_functioncalmodulin binding
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0006816biological_processcalcium ion transport
E0016020cellular_componentmembrane
E0016324cellular_componentapical plasma membrane
E0034220biological_processmonoatomic ion transmembrane transport
E0035809biological_processregulation of urine volume
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
E0051289biological_processprotein homotetramerization
E0055074biological_processcalcium ion homeostasis
E0055085biological_processtransmembrane transport
E0070588biological_processcalcium ion transmembrane transport
E0097553biological_processcalcium ion transmembrane import into cytosol
E0098703biological_processcalcium ion import across plasma membrane
F0000922cellular_componentspindle pole
F0005509molecular_functioncalcium ion binding
F0005513biological_processdetection of calcium ion
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005813cellular_componentcentrosome
F0005819cellular_componentspindle
F0005829cellular_componentcytosol
F0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
F0019904molecular_functionprotein domain specific binding
F0032991cellular_componentprotein-containing complex
F0043209cellular_componentmyelin sheath
F0046872molecular_functionmetal ion binding
F0097720biological_processcalcineurin-mediated signaling
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA F 201
ChainResidue
FASP129
FASP131
FASP133
FGLN135
FASN137
site_idAC2
Number of Residues6
Detailsbinding site for residue CA F 202
ChainResidue
FILE100
FGLU104
FASP93
FASP95
FASN97
FTYR99
site_idAC3
Number of Residues4
Detailsbinding site for residue CA F 203
ChainResidue
FASP20
FGLY25
FTHR26
FGLU31
site_idAC4
Number of Residues6
Detailsbinding site for residue CA F 204
ChainResidue
FASP56
FASP58
FASN60
FTHR62
FASP64
FGLU67
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
FASP20-LEU32
FASP56-PHE68
FASP93-LEU105
FASP129-PHE141
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues496
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"29323279","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues164
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29323279","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues128
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29323279","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues80
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"PubMed","id":"29323279","evidenceCode":"ECO:0000269"}]}
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 Residues132
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 Residues16
DetailsRegion: {"description":"Interaction with S100A10","evidences":[{"source":"UniProtKB","id":"P69744","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsRegion: {"description":"Involved in Ca(2+)-dependent inactivation","evidences":[{"source":"PubMed","id":"12634930","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29323279","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues32
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7356670","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"9716384","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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