8SI8
Cryo-EM structure of TRPM7 N1098Q mutant in GDN detergent in complex with inhibitor VER155008 in closed state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0016020 | cellular_component | membrane |
A | 0051262 | biological_process | protein tetramerization |
A | 0055085 | biological_process | transmembrane transport |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0016020 | cellular_component | membrane |
B | 0051262 | biological_process | protein tetramerization |
B | 0055085 | biological_process | transmembrane transport |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0016020 | cellular_component | membrane |
C | 0051262 | biological_process | protein tetramerization |
C | 0055085 | biological_process | transmembrane transport |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0016020 | cellular_component | membrane |
D | 0051262 | biological_process | protein tetramerization |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 100 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | ALA851-VAL876 | |
B | ALA851-VAL876 | |
C | ALA851-VAL876 | |
D | ALA851-VAL876 |
site_id | SWS_FT_FI2 |
Number of Residues | 80 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | LYS877-PRO882 | |
C | GLY944-HIS956 | |
C | PRO1024-HIS1025 | |
C | GLY1067-GLY1069 | |
D | LYS877-PRO882 | |
D | GLY944-HIS956 | |
D | PRO1024-HIS1025 | |
D | GLY1067-GLY1069 | |
A | GLY944-HIS956 | |
A | PRO1024-HIS1025 | |
A | GLY1067-GLY1069 | |
B | LYS877-PRO882 | |
B | GLY944-HIS956 | |
B | PRO1024-HIS1025 | |
B | GLY1067-GLY1069 | |
C | LYS877-PRO882 |
site_id | SWS_FT_FI3 |
Number of Residues | 84 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | SER883-VAL904 | |
B | SER883-VAL904 | |
C | SER883-VAL904 | |
D | SER883-VAL904 |
site_id | SWS_FT_FI4 |
Number of Residues | 144 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | PHE905-TYR923 | |
A | ALA981-ASN999 | |
B | PHE905-TYR923 | |
B | ALA981-ASN999 | |
C | PHE905-TYR923 | |
C | ALA981-ASN999 | |
D | PHE905-TYR923 | |
D | ALA981-ASN999 |
site_id | SWS_FT_FI5 |
Number of Residues | 76 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | PHE924-PHE943 | |
B | PHE924-PHE943 | |
C | PHE924-PHE943 | |
D | PHE924-PHE943 |
site_id | SWS_FT_FI6 |
Number of Residues | 92 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | VAL957-LEU980 | |
B | VAL957-LEU980 | |
C | VAL957-LEU980 | |
D | VAL957-LEU980 |
site_id | SWS_FT_FI7 |
Number of Residues | 92 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | MET1000-TYR1023 | |
B | MET1000-TYR1023 | |
C | MET1000-TYR1023 | |
D | MET1000-TYR1023 |
site_id | SWS_FT_FI8 |
Number of Residues | 160 |
Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | GLU1026-CYS1066 | |
B | GLU1026-CYS1066 | |
C | GLU1026-CYS1066 | |
D | GLU1026-CYS1066 |
site_id | SWS_FT_FI9 |
Number of Residues | 112 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:37156763, ECO:0007744|PDB:8SI2 |
Chain | Residue | Details |
A | THR1070-GLN1098 | |
B | THR1070-GLN1098 | |
C | THR1070-GLN1098 | |
D | THR1070-GLN1098 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q96QT4 |
Chain | Residue | Details |
A | SER101 | |
C | SER1191 | |
C | SER1193 | |
C | SER1258 | |
D | SER101 | |
D | SER1191 | |
D | SER1193 | |
D | SER1258 | |
A | SER1191 | |
A | SER1193 | |
A | SER1258 | |
B | SER101 | |
B | SER1191 | |
B | SER1193 | |
B | SER1258 | |
C | SER101 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q96QT4 |
Chain | Residue | Details |
A | THR1163 | |
A | THR1265 | |
B | THR1163 | |
B | THR1265 | |
C | THR1163 | |
C | THR1265 | |
D | THR1163 | |
D | THR1265 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:22222377 |
Chain | Residue | Details |
A | SER1224 | |
B | SER1224 | |
C | SER1224 | |
D | SER1224 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER1255 | |
B | SER1255 | |
C | SER1255 | |
D | SER1255 |
site_id | SWS_FT_FI14 |
Number of Residues | 12 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q96QT4 |
Chain | Residue | Details |
A | CYS1143 | |
D | CYS1143 | |
D | CYS1144 | |
D | CYS1146 | |
A | CYS1144 | |
A | CYS1146 | |
B | CYS1143 | |
B | CYS1144 | |
B | CYS1146 | |
C | CYS1143 | |
C | CYS1144 | |
C | CYS1146 |