6PZC
Cryo-EM structure of the pancreatic beta-cell SUR1 bound to carbamazepine
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0000166 | molecular_function | nucleotide binding |
H | 0005267 | molecular_function | potassium channel activity |
H | 0005524 | molecular_function | ATP binding |
H | 0005886 | cellular_component | plasma membrane |
H | 0006813 | biological_process | potassium ion transport |
H | 0008281 | molecular_function | sulfonylurea receptor activity |
H | 0009410 | biological_process | response to xenobiotic stimulus |
H | 0016020 | cellular_component | membrane |
H | 0016887 | molecular_function | ATP hydrolysis activity |
H | 0022857 | molecular_function | transmembrane transporter activity |
H | 0032991 | cellular_component | protein-containing complex |
H | 0033198 | biological_process | response to ATP |
H | 0042383 | cellular_component | sarcolemma |
H | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
H | 0046872 | molecular_function | metal ion binding |
H | 0055085 | biological_process | transmembrane transport |
H | 0071805 | biological_process | potassium ion transmembrane transport |
H | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRISVARAL |
Chain | Residue | Details |
H | LEU830-LEU844 | |
H | PHE1482-PHE1496 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 110 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:10506167 |
Chain | Residue | Details |
H | MET1-ALA30 | |
H | ALA90-LEU106 | |
H | PHE154-PHE169 | |
H | TYR1032-VAL1067 | |
H | THR1266-VAL1281 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | LEU31-LEU47 |
site_id | SWS_FT_FI3 |
Number of Residues | 856 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:10506167 |
Chain | Residue | Details |
H | PHE48-ASN72 | |
H | TYR124-LEU136 | |
H | VAL187-SER303 | |
H | LEU593-LEU1013 | |
H | MET1298-LYS1582 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | LEU73-ILE89 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | TYR107-TYR123 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | ILE137-LYS153 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | CYS170-GLU186 |
site_id | SWS_FT_FI8 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | THR304-CYS319 |
site_id | SWS_FT_FI9 |
Number of Residues | 60 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
H | ILE320-TYR356 | |
H | ILE455-ALA460 | |
H | THR558-ALA576 | |
H | PRO1162 |
site_id | SWS_FT_FI10 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | VAL357-PHE372 |
site_id | SWS_FT_FI11 |
Number of Residues | 263 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
H | LEU373-LEU438 | |
H | GLN474-SER541 | |
H | THR1085-LEU1143 | |
H | TYR1176-GLU1249 |
site_id | SWS_FT_FI12 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | TRP439-TYR454 |
site_id | SWS_FT_FI13 |
Number of Residues | 12 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | LEU461-VAL473 |
site_id | SWS_FT_FI14 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | ILE542-ILE557 |
site_id | SWS_FT_FI15 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=11 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | PHE577-LEU592 |
site_id | SWS_FT_FI16 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=12 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | SER1014-ASP1031 |
site_id | SWS_FT_FI17 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=13 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | PHE1068-VAL1084 |
site_id | SWS_FT_FI18 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=14 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | SER1144-THR1161 |
site_id | SWS_FT_FI19 |
Number of Residues | 12 |
Details | TRANSMEM: Helical; Name=15 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | VAL1163-CYS1175 |
site_id | SWS_FT_FI20 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=16 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | VAL1250-ALA1265 |
site_id | SWS_FT_FI21 |
Number of Residues | 15 |
Details | TRANSMEM: Helical; Name=17 => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | GLY1282-TRP1297 |
site_id | SWS_FT_FI22 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q09428 |
Chain | Residue | Details |
H | TRP688 | |
H | SER1386 | |
H | SER1387 | |
H | SER1483 | |
H | GLY716 | |
H | SER720 | |
H | SER721 | |
H | GLN775 | |
H | THR1381 | |
H | GLY1382 | |
H | GLY1384 | |
H | LYS1385 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10506167, ECO:0000269|PubMed:8942641 |
Chain | Residue | Details |
H | ASN10 |
site_id | SWS_FT_FI24 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10506167 |
Chain | Residue | Details |
H | ASN1050 |