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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6DRJ

Structure of TRPM2 ion channel receptor by single particle electron cryo-microscopy, ADPR/Ca2+ bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0016020cellular_componentmembrane
A0019722biological_processcalcium-mediated signaling
A0034220biological_processmonoatomic ion transmembrane transport
A0046872molecular_functionmetal ion binding
A0047631molecular_functionADP-ribose diphosphatase activity
A0051289biological_processprotein homotetramerization
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
A0072570molecular_functionADP-D-ribose binding
A0072571molecular_functionmono-ADP-D-ribose binding
A0099094molecular_functionligand-gated monoatomic cation channel activity
A0099604molecular_functionligand-gated calcium channel activity
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006816biological_processcalcium ion transport
B0016020cellular_componentmembrane
B0019722biological_processcalcium-mediated signaling
B0034220biological_processmonoatomic ion transmembrane transport
B0046872molecular_functionmetal ion binding
B0047631molecular_functionADP-ribose diphosphatase activity
B0051289biological_processprotein homotetramerization
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
B0072570molecular_functionADP-D-ribose binding
B0072571molecular_functionmono-ADP-D-ribose binding
B0099094molecular_functionligand-gated monoatomic cation channel activity
B0099604molecular_functionligand-gated calcium channel activity
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0016020cellular_componentmembrane
C0019722biological_processcalcium-mediated signaling
C0034220biological_processmonoatomic ion transmembrane transport
C0046872molecular_functionmetal ion binding
C0047631molecular_functionADP-ribose diphosphatase activity
C0051289biological_processprotein homotetramerization
C0055085biological_processtransmembrane transport
C0070588biological_processcalcium ion transmembrane transport
C0072570molecular_functionADP-D-ribose binding
C0072571molecular_functionmono-ADP-D-ribose binding
C0099094molecular_functionligand-gated monoatomic cation channel activity
C0099604molecular_functionligand-gated calcium channel activity
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006816biological_processcalcium ion transport
D0016020cellular_componentmembrane
D0019722biological_processcalcium-mediated signaling
D0034220biological_processmonoatomic ion transmembrane transport
D0046872molecular_functionmetal ion binding
D0047631molecular_functionADP-ribose diphosphatase activity
D0051289biological_processprotein homotetramerization
D0055085biological_processtransmembrane transport
D0070588biological_processcalcium ion transmembrane transport
D0072570molecular_functionADP-D-ribose binding
D0072571molecular_functionmono-ADP-D-ribose binding
D0099094molecular_functionligand-gated monoatomic cation channel activity
D0099604molecular_functionligand-gated calcium channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue APR A 2001
ChainResidue
ATHR150
AGLY309
APRO310
AGLY311
ATHR312
AARG334
AGLY151
AGLY152
AALA153
ALYS154
AASN155
ATHR186
ATYR271
AARG278
site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 2002
ChainResidue
AGLU857
AGLN860
AASN883
AASP886
AGLU1088
site_idAC3
Number of Residues14
Detailsbinding site for residue APR B 2001
ChainResidue
BTHR150
BGLY151
BGLY152
BALA153
BLYS154
BASN155
BTHR186
BTYR271
BARG278
BGLY309
BPRO310
BGLY311
BTHR312
BARG334
site_idAC4
Number of Residues5
Detailsbinding site for residue CA B 2002
ChainResidue
BGLU857
BGLN860
BASN883
BASP886
BGLU1088
site_idAC5
Number of Residues14
Detailsbinding site for residue APR C 2001
ChainResidue
CTHR150
CGLY151
CGLY152
CALA153
CLYS154
CASN155
CTHR186
CTYR271
CARG278
CGLY309
CPRO310
CGLY311
CTHR312
CARG334
site_idAC6
Number of Residues5
Detailsbinding site for residue CA C 2002
ChainResidue
CGLU857
CGLN860
CASN883
CASP886
CGLU1088
site_idAC7
Number of Residues14
Detailsbinding site for residue APR D 2001
ChainResidue
DTHR150
DGLY151
DGLY152
DALA153
DLYS154
DASN155
DTHR186
DTYR271
DARG278
DGLY309
DPRO310
DGLY311
DTHR312
DARG334
site_idAC8
Number of Residues5
Detailsbinding site for residue CA D 2002
ChainResidue
DGLU857
DGLN860
DASN883
DASP886
DGLU1088
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsIntramembrane: {"evidences":[{"source":"PubMed","id":"30250252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues520
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30250252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues208
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues236
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues96
DetailsIntramembrane: {"description":"Pore-forming","evidences":[{"source":"PubMed","id":"30250252","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsMotif: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"30250252","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30250252","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O94759","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-14

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