6DRJ
Structure of TRPM2 ion channel receptor by single particle electron cryo-microscopy, ADPR/Ca2+ bound state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005262 | molecular_function | calcium channel activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0016020 | cellular_component | membrane |
A | 0019722 | biological_process | calcium-mediated signaling |
A | 0046872 | molecular_function | metal ion binding |
A | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
A | 0051289 | biological_process | protein homotetramerization |
A | 0055085 | biological_process | transmembrane transport |
A | 0070588 | biological_process | calcium ion transmembrane transport |
A | 0072570 | molecular_function | ADP-D-ribose binding |
A | 0072571 | molecular_function | mono-ADP-D-ribose binding |
A | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
A | 0099604 | molecular_function | ligand-gated calcium channel activity |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005262 | molecular_function | calcium channel activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0016020 | cellular_component | membrane |
B | 0019722 | biological_process | calcium-mediated signaling |
B | 0046872 | molecular_function | metal ion binding |
B | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
B | 0051289 | biological_process | protein homotetramerization |
B | 0055085 | biological_process | transmembrane transport |
B | 0070588 | biological_process | calcium ion transmembrane transport |
B | 0072570 | molecular_function | ADP-D-ribose binding |
B | 0072571 | molecular_function | mono-ADP-D-ribose binding |
B | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
B | 0099604 | molecular_function | ligand-gated calcium channel activity |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005262 | molecular_function | calcium channel activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0016020 | cellular_component | membrane |
C | 0019722 | biological_process | calcium-mediated signaling |
C | 0046872 | molecular_function | metal ion binding |
C | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
C | 0051289 | biological_process | protein homotetramerization |
C | 0055085 | biological_process | transmembrane transport |
C | 0070588 | biological_process | calcium ion transmembrane transport |
C | 0072570 | molecular_function | ADP-D-ribose binding |
C | 0072571 | molecular_function | mono-ADP-D-ribose binding |
C | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
C | 0099604 | molecular_function | ligand-gated calcium channel activity |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0005262 | molecular_function | calcium channel activity |
D | 0005509 | molecular_function | calcium ion binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0016020 | cellular_component | membrane |
D | 0019722 | biological_process | calcium-mediated signaling |
D | 0046872 | molecular_function | metal ion binding |
D | 0047631 | molecular_function | ADP-ribose diphosphatase activity |
D | 0051289 | biological_process | protein homotetramerization |
D | 0055085 | biological_process | transmembrane transport |
D | 0070588 | biological_process | calcium ion transmembrane transport |
D | 0072570 | molecular_function | ADP-D-ribose binding |
D | 0072571 | molecular_function | mono-ADP-D-ribose binding |
D | 0099094 | molecular_function | ligand-gated monoatomic cation channel activity |
D | 0099604 | molecular_function | ligand-gated calcium channel activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue APR A 2001 |
Chain | Residue |
A | THR150 |
A | GLY309 |
A | PRO310 |
A | GLY311 |
A | THR312 |
A | ARG334 |
A | GLY151 |
A | GLY152 |
A | ALA153 |
A | LYS154 |
A | ASN155 |
A | THR186 |
A | TYR271 |
A | ARG278 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA A 2002 |
Chain | Residue |
A | GLU857 |
A | GLN860 |
A | ASN883 |
A | ASP886 |
A | GLU1088 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue APR B 2001 |
Chain | Residue |
B | THR150 |
B | GLY151 |
B | GLY152 |
B | ALA153 |
B | LYS154 |
B | ASN155 |
B | THR186 |
B | TYR271 |
B | ARG278 |
B | GLY309 |
B | PRO310 |
B | GLY311 |
B | THR312 |
B | ARG334 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA B 2002 |
Chain | Residue |
B | GLU857 |
B | GLN860 |
B | ASN883 |
B | ASP886 |
B | GLU1088 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue APR C 2001 |
Chain | Residue |
C | THR150 |
C | GLY151 |
C | GLY152 |
C | ALA153 |
C | LYS154 |
C | ASN155 |
C | THR186 |
C | TYR271 |
C | ARG278 |
C | GLY309 |
C | PRO310 |
C | GLY311 |
C | THR312 |
C | ARG334 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue CA C 2002 |
Chain | Residue |
C | GLU857 |
C | GLN860 |
C | ASN883 |
C | ASP886 |
C | GLU1088 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue APR D 2001 |
Chain | Residue |
D | THR150 |
D | GLY151 |
D | GLY152 |
D | ALA153 |
D | LYS154 |
D | ASN155 |
D | THR186 |
D | TYR271 |
D | ARG278 |
D | GLY309 |
D | PRO310 |
D | GLY311 |
D | THR312 |
D | ARG334 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CA D 2002 |
Chain | Residue |
D | GLU857 |
D | GLN860 |
D | ASN883 |
D | ASP886 |
D | GLU1088 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 116 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:30250252 |
Chain | Residue | Details |
A | LYS730-TYR742 | |
A | PRO1093-ARG1110 | |
B | LYS730-TYR742 | |
B | PRO1093-ARG1110 | |
C | LYS730-TYR742 | |
C | PRO1093-ARG1110 | |
D | LYS730-TYR742 | |
D | PRO1093-ARG1110 |
site_id | SWS_FT_FI2 |
Number of Residues | 1968 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | THR743-PHE813 | |
C | THR743-PHE813 | |
C | HIS863-LEU881 | |
C | ILE932-MET946 | |
C | TYR1065-ARG1092 | |
D | THR743-PHE813 | |
D | HIS863-LEU881 | |
D | ILE932-MET946 | |
D | TYR1065-ARG1092 | |
A | HIS863-LEU881 | |
A | ILE932-MET946 | |
A | TYR1065-ARG1092 | |
B | THR743-PHE813 | |
B | HIS863-LEU881 | |
B | ILE932-MET946 | |
B | TYR1065-ARG1092 |
site_id | SWS_FT_FI3 |
Number of Residues | 520 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:30250252 |
Chain | Residue | Details |
A | TYR814-ASP834 | |
B | GLY911-SER931 | |
B | MET947-ILE973 | |
B | THR1040-ASN1064 | |
C | TYR814-ASP834 | |
C | ARG842-TYR862 | |
C | TRP882-GLN902 | |
C | GLY911-SER931 | |
C | MET947-ILE973 | |
C | THR1040-ASN1064 | |
D | TYR814-ASP834 | |
A | ARG842-TYR862 | |
D | ARG842-TYR862 | |
D | TRP882-GLN902 | |
D | GLY911-SER931 | |
D | MET947-ILE973 | |
D | THR1040-ASN1064 | |
A | TRP882-GLN902 | |
A | GLY911-SER931 | |
A | MET947-ILE973 | |
A | THR1040-ASN1064 | |
B | TYR814-ASP834 | |
B | ARG842-TYR862 | |
B | TRP882-GLN902 |
site_id | SWS_FT_FI4 |
Number of Residues | 208 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | PHE835-TRP841 | |
C | ALA903-ILE910 | |
C | GLU974-ILE982 | |
C | ASP1008-LEU1039 | |
D | PHE835-TRP841 | |
D | ALA903-ILE910 | |
D | GLU974-ILE982 | |
D | ASP1008-LEU1039 | |
A | ALA903-ILE910 | |
A | GLU974-ILE982 | |
A | ASP1008-LEU1039 | |
B | PHE835-TRP841 | |
B | ALA903-ILE910 | |
B | GLU974-ILE982 | |
B | ASP1008-LEU1039 | |
C | PHE835-TRP841 |
site_id | SWS_FT_FI5 |
Number of Residues | 96 |
Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:30250252 |
Chain | Residue | Details |
A | ILE983-PHE1007 | |
B | ILE983-PHE1007 | |
C | ILE983-PHE1007 | |
D | ILE983-PHE1007 |
site_id | SWS_FT_FI6 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30250252 |
Chain | Residue | Details |
A | TYR271 | |
B | ARG278 | |
B | GLY309 | |
B | ARG334 | |
B | ILE858 | |
B | LEU861 | |
B | ILE884 | |
B | TYR1089 | |
C | TYR271 | |
C | ARG278 | |
C | GLY309 | |
A | ARG278 | |
C | ARG334 | |
C | ILE858 | |
C | LEU861 | |
C | ILE884 | |
C | TYR1089 | |
D | TYR271 | |
D | ARG278 | |
D | GLY309 | |
D | ARG334 | |
D | ILE858 | |
A | GLY309 | |
D | LEU861 | |
D | ILE884 | |
D | TYR1089 | |
A | ARG334 | |
A | ILE858 | |
A | LEU861 | |
A | ILE884 | |
A | TYR1089 | |
B | TYR271 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ALA1016 | |
B | ALA1016 | |
C | ALA1016 | |
D | ALA1016 |