6BWI
3.7 angstrom cryoEM structure of full length human TRPM4
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 | 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 | 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 | 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 | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 492 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581 |
Chain | Residue | Details |
A | PHE783-VAL803 | |
B | LEU887-PHE910 | |
B | PHE931-LEU951 | |
B | VAL1020-ILE1040 | |
C | PHE783-VAL803 | |
C | LEU815-GLY835 | |
C | TRP864-THR884 | |
C | LEU887-PHE910 | |
C | PHE931-LEU951 | |
C | VAL1020-ILE1040 | |
D | PHE783-VAL803 | |
A | LEU815-GLY835 | |
D | LEU815-GLY835 | |
D | TRP864-THR884 | |
D | LEU887-PHE910 | |
D | PHE931-LEU951 | |
D | VAL1020-ILE1040 | |
A | TRP864-THR884 | |
A | LEU887-PHE910 | |
A | PHE931-LEU951 | |
A | VAL1020-ILE1040 | |
B | PHE783-VAL803 | |
B | LEU815-GLY835 | |
B | TRP864-THR884 |
site_id | SWS_FT_FI2 |
Number of Residues | 224 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581 |
Chain | Residue | Details |
A | ASP804-GLU814 | |
C | PRO885-GLY886 | |
C | LEU952-LEU963 | |
C | VAL985-LEU1019 | |
D | ASP804-GLU814 | |
D | PRO885-GLY886 | |
D | LEU952-LEU963 | |
D | VAL985-LEU1019 | |
A | PRO885-GLY886 | |
A | LEU952-LEU963 | |
A | VAL985-LEU1019 | |
B | ASP804-GLU814 | |
B | PRO885-GLY886 | |
B | LEU952-LEU963 | |
B | VAL985-LEU1019 | |
C | ASP804-GLU814 |
site_id | SWS_FT_FI3 |
Number of Residues | 184 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581 |
Chain | Residue | Details |
A | GLY836-SER863 | |
A | THR911-VAL930 | |
B | GLY836-SER863 | |
B | THR911-VAL930 | |
C | GLY836-SER863 | |
C | THR911-VAL930 | |
D | GLY836-SER863 | |
D | THR911-VAL930 |
site_id | SWS_FT_FI4 |
Number of Residues | 80 |
Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581 |
Chain | Residue | Details |
A | ARG964-ASP984 | |
B | ARG964-ASP984 | |
C | ARG964-ASP984 | |
D | ARG964-ASP984 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:Q7TN37 |
Chain | Residue | Details |
A | ARG421 | |
A | GLY448 | |
B | ARG421 | |
B | GLY448 | |
C | ARG421 | |
C | GLY448 | |
D | ARG421 | |
D | GLY448 |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29217581, ECO:0007744|PDB:6BQV |
Chain | Residue | Details |
A | GLU828 | |
D | GLU828 | |
D | GLN831 | |
D | ASN865 | |
A | GLN831 | |
A | ASN865 | |
B | GLU828 | |
B | GLN831 | |
B | ASN865 | |
C | GLU828 | |
C | GLN831 | |
C | ASN865 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:29217581, ECO:0007744|PDB:6BQV |
Chain | Residue | Details |
A | ASP868 | |
B | ASP868 | |
C | ASP868 | |
D | ASP868 |
site_id | SWS_FT_FI8 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000305|PubMed:15590641 |
Chain | Residue | Details |
A | SER1145 | |
A | SER1152 | |
B | SER1145 | |
B | SER1152 | |
C | SER1145 | |
C | SER1152 | |
D | SER1145 | |
D | SER1152 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29217581 |
Chain | Residue | Details |
A | ASN992 | |
B | ASN992 | |
C | ASN992 | |
D | ASN992 |