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6UY0

Cryo-EM structure of wild-type bovine multidrug resistance protein 1 (MRP1) under active turnover conditions

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009410biological_processresponse to xenobiotic stimulus
A0015431molecular_functionABC-type glutathione S-conjugate transporter activity
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0022857molecular_functiontransmembrane transporter activity
A0034634molecular_functionglutathione transmembrane transporter activity
A0034775biological_processglutathione transmembrane transport
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0050729biological_processpositive regulation of inflammatory response
A0055085biological_processtransmembrane transport
A0070729biological_processcyclic nucleotide transport
A0071716biological_processleukotriene transport
A0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue ATP A 1601
ChainResidue
AASN412
AGLN713
AHIS827
APHE1410
AGLU1427
AASN1428
ALEU1429
ASER1430
AGLY1432
AGLN1433
AMG1603
ATRP653
AVAL680
AGLY681
ACYS682
AGLY683
ALYS684
ASER685
ASER686

site_idAC2
Number of Residues13
Detailsbinding site for residue ADP A 1602
ChainResidue
AASN767
ASER769
AGLN772
AGLU1064
ATYR1301
AVAL1308
AGLY1329
AALA1330
AGLY1331
ALYS1332
ASER1333
ASER1334
AMG1604

site_idAC3
Number of Residues3
Detailsbinding site for residue MG A 1603
ChainResidue
ASER685
AGLN713
AATP1601

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 1604
ChainResidue
ASER1333
AGLN1374
AADP1602

site_idAC5
Number of Residues3
Detailsbinding site for residue CLR A 1605
ChainResidue
ATYR544
ALEU976
ATHR1028

site_idAC6
Number of Residues6
Detailsbinding site for residue CLR A 1606
ChainResidue
AMET966
AILE1090
AARG1130
ASER1250
AMET1253
AGLU1254

site_idAC7
Number of Residues3
Detailsbinding site for residue CLR A 1607
ChainResidue
ALYS488
AILE603
AILE606

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRVSLARAV
ChainResidueDetails
ALEU768-VAL782
ALEU1429-LEU1443

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues139
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
AMET1-PHE33
AARG96-LYS100
ASER155-ASP172
AMET338-GLY363
ALEU462-PRO464
AVAL569-ASN590
ASER988-SER1024
AALA1110
ALEU1224-SER1225

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLN34-PHE54

site_idSWS_FT_FI3
Number of Residues1017
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
ALEU55-LYS74
APHE122-GLN133
AARG194-VAL316
APHE385-TYR440
ALYS486-ALA547
ASER612-MET966
AARG1046-GLN1088
ATYR1132-LEU1202
AVAL1247-VAL1530

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATHR75-GLU95

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU101-THR121

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ASER134-ARG154

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AVAL173-ASP193

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU317-LEU337

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATYR364-TYR384

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AILE441-ASN461

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ASER465-MET485

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AVAL548-TYR568

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AILE591-VAL611

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALYS967-ALA987

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=13 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLN1025-ARG1045

site_idSWS_FT_FI16
Number of Residues20
DetailsTRANSMEM: Helical; Name=14 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AVAL1089-LEU1109

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=15 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATHR1111-PHE1131

site_idSWS_FT_FI18
Number of Residues20
DetailsTRANSMEM: Helical; Name=16 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLU1203-SER1223

site_idSWS_FT_FI19
Number of Residues20
DetailsTRANSMEM: Helical; Name=17 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AALA1226-LEU1246

site_idSWS_FT_FI20
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY678
AGLY1326

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O35379
ChainResidueDetails
ATYR277

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O35379
ChainResidueDetails
ASER289

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O35379
ChainResidueDetails
ALYS503

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P33527
ChainResidueDetails
ASER915
ASER930

site_idSWS_FT_FI25
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN19
AASN1005

218853

PDB entries from 2024-04-24

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