6UY0
Cryo-EM structure of wild-type bovine multidrug resistance protein 1 (MRP1) under active turnover conditions
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006869 | biological_process | lipid transport |
A | 0008559 | molecular_function | ABC-type xenobiotic transporter activity |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0015431 | molecular_function | ABC-type glutathione S-conjugate transporter activity |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0034634 | molecular_function | glutathione transmembrane transporter activity |
A | 0034775 | biological_process | glutathione transmembrane transport |
A | 0042908 | biological_process | xenobiotic transport |
A | 0042910 | molecular_function | xenobiotic transmembrane transporter activity |
A | 0050729 | biological_process | positive regulation of inflammatory response |
A | 0055085 | biological_process | transmembrane transport |
A | 0070729 | biological_process | cyclic nucleotide transport |
A | 0071716 | biological_process | leukotriene transport |
A | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue ATP A 1601 |
Chain | Residue |
A | ASN412 |
A | GLN713 |
A | HIS827 |
A | PHE1410 |
A | GLU1427 |
A | ASN1428 |
A | LEU1429 |
A | SER1430 |
A | GLY1432 |
A | GLN1433 |
A | MG1603 |
A | TRP653 |
A | VAL680 |
A | GLY681 |
A | CYS682 |
A | GLY683 |
A | LYS684 |
A | SER685 |
A | SER686 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue ADP A 1602 |
Chain | Residue |
A | ASN767 |
A | SER769 |
A | GLN772 |
A | GLU1064 |
A | TYR1301 |
A | VAL1308 |
A | GLY1329 |
A | ALA1330 |
A | GLY1331 |
A | LYS1332 |
A | SER1333 |
A | SER1334 |
A | MG1604 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue MG A 1603 |
Chain | Residue |
A | SER685 |
A | GLN713 |
A | ATP1601 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue MG A 1604 |
Chain | Residue |
A | SER1333 |
A | GLN1374 |
A | ADP1602 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CLR A 1605 |
Chain | Residue |
A | TYR544 |
A | LEU976 |
A | THR1028 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CLR A 1606 |
Chain | Residue |
A | MET966 |
A | ILE1090 |
A | ARG1130 |
A | SER1250 |
A | MET1253 |
A | GLU1254 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CLR A 1607 |
Chain | Residue |
A | LYS488 |
A | ILE603 |
A | ILE606 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAV |
Chain | Residue | Details |
A | LEU768-VAL782 | |
A | LEU1429-LEU1443 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 139 |
Details | TOPO_DOM: Extracellular => ECO:0000250 |
Chain | Residue | Details |
A | MET1-PHE33 | |
A | ARG96-LYS100 | |
A | SER155-ASP172 | |
A | MET338-GLY363 | |
A | LEU462-PRO464 | |
A | VAL569-ASN590 | |
A | SER988-SER1024 | |
A | ALA1110 | |
A | LEU1224-SER1225 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | GLN34-PHE54 |
site_id | SWS_FT_FI3 |
Number of Residues | 1017 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
Chain | Residue | Details |
A | LEU55-LYS74 | |
A | PHE122-GLN133 | |
A | ARG194-VAL316 | |
A | PHE385-TYR440 | |
A | LYS486-ALA547 | |
A | SER612-MET966 | |
A | ARG1046-GLN1088 | |
A | TYR1132-LEU1202 | |
A | VAL1247-VAL1530 |
site_id | SWS_FT_FI4 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | THR75-GLU95 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | LEU101-THR121 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | SER134-ARG154 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | VAL173-ASP193 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | LEU317-LEU337 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | TYR364-TYR384 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | ILE441-ASN461 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | SER465-MET485 |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=10 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | VAL548-TYR568 |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=11 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | ILE591-VAL611 |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=12 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | LYS967-ALA987 |
site_id | SWS_FT_FI15 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=13 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | GLN1025-ARG1045 |
site_id | SWS_FT_FI16 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=14 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | VAL1089-LEU1109 |
site_id | SWS_FT_FI17 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=15 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | THR1111-PHE1131 |
site_id | SWS_FT_FI18 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=16 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | GLU1203-SER1223 |
site_id | SWS_FT_FI19 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=17 => ECO:0000255|PROSITE-ProRule:PRU00441 |
Chain | Residue | Details |
A | ALA1226-LEU1246 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434 |
Chain | Residue | Details |
A | GLY678 | |
A | GLY1326 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O35379 |
Chain | Residue | Details |
A | TYR277 |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O35379 |
Chain | Residue | Details |
A | SER289 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O35379 |
Chain | Residue | Details |
A | LYS503 |
site_id | SWS_FT_FI24 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P33527 |
Chain | Residue | Details |
A | SER915 | |
A | SER930 |
site_id | SWS_FT_FI25 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN19 | |
A | ASN1005 |