Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
A0016020cellular_componentmembrane
A0019722biological_processcalcium-mediated signaling
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
B0016020cellular_componentmembrane
B0019722biological_processcalcium-mediated signaling
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
C0016020cellular_componentmembrane
C0019722biological_processcalcium-mediated signaling
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
D0016020cellular_componentmembrane
D0019722biological_processcalcium-mediated signaling
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
DetailsINTRAMEM: INTRAMEM => ECO:0000269|PubMed:30250252
ChainResidueDetails
ALYS730-TYR742
APRO1093-ARG1110
BLYS730-TYR742
BPRO1093-ARG1110
CLYS730-TYR742
CPRO1093-ARG1110
DLYS730-TYR742
DPRO1093-ARG1110

site_idSWS_FT_FI2
Number of Residues1968
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
ATHR743-PHE813
CTHR743-PHE813
CHIS863-LEU881
CILE932-MET946
CTYR1065-ARG1092
DTHR743-PHE813
DHIS863-LEU881
DILE932-MET946
DTYR1065-ARG1092
AHIS863-LEU881
AILE932-MET946
ATYR1065-ARG1092
BTHR743-PHE813
BHIS863-LEU881
BILE932-MET946
BTYR1065-ARG1092

site_idSWS_FT_FI3
Number of Residues520
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:30250252
ChainResidueDetails
ATYR814-ASP834
BGLY911-SER931
BMET947-ILE973
BTHR1040-ASN1064
CTYR814-ASP834
CARG842-TYR862
CTRP882-GLN902
CGLY911-SER931
CMET947-ILE973
CTHR1040-ASN1064
DTYR814-ASP834
AARG842-TYR862
DARG842-TYR862
DTRP882-GLN902
DGLY911-SER931
DMET947-ILE973
DTHR1040-ASN1064
ATRP882-GLN902
AGLY911-SER931
AMET947-ILE973
ATHR1040-ASN1064
BTYR814-ASP834
BARG842-TYR862
BTRP882-GLN902

site_idSWS_FT_FI4
Number of Residues208
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
APHE835-TRP841
CALA903-ILE910
CGLU974-ILE982
CASP1008-LEU1039
DPHE835-TRP841
DALA903-ILE910
DGLU974-ILE982
DASP1008-LEU1039
AALA903-ILE910
AGLU974-ILE982
AASP1008-LEU1039
BPHE835-TRP841
BALA903-ILE910
BGLU974-ILE982
BASP1008-LEU1039
CPHE835-TRP841

site_idSWS_FT_FI5
Number of Residues96
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:30250252
ChainResidueDetails
AILE983-PHE1007
BILE983-PHE1007
CILE983-PHE1007
DILE983-PHE1007

site_idSWS_FT_FI6
Number of Residues32
DetailsBINDING: BINDING => ECO:0000305|PubMed:30250252
ChainResidueDetails
ATYR271
BARG278
BGLY309
BARG334
BILE858
BLEU861
BILE884
BTYR1089
CTYR271
CARG278
CGLY309
AARG278
CARG334
CILE858
CLEU861
CILE884
CTYR1089
DTYR271
DARG278
DGLY309
DARG334
DILE858
AGLY309
DLEU861
DILE884
DTYR1089
AARG334
AILE858
ALEU861
AILE884
ATYR1089
BTYR271

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AALA1016
BALA1016
CALA1016
DALA1016

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon