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8HW2

Cryo-EM structure of beta-estradiol 17-(beta-D-glucuronide)-bound human ABC transporter ABCC3 in nanodiscs

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006805biological_processxenobiotic metabolic process
A0006855biological_processxenobiotic transmembrane transport
A0006869biological_processlipid transport
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009925cellular_componentbasal plasma membrane
A0015164molecular_functionglucuronoside transmembrane transporter activity
A0015431molecular_functionABC-type glutathione S-conjugate transporter activity
A0015432molecular_functionABC-type bile acid transporter activity
A0015721biological_processbile acid and bile salt transport
A0015779biological_processglucuronoside transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0022857molecular_functiontransmembrane transporter activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0043225molecular_functionATPase-coupled inorganic anion transmembrane transporter activity
A0055085biological_processtransmembrane transport
A0071714molecular_functionicosanoid transmembrane transporter activity
A0071716biological_processleukotriene transport
A0098656biological_processmonoatomic anion transmembrane transport
A0140359molecular_functionABC-type transporter activity
A0150104biological_processtransport across blood-brain barrier
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRVSLARAV
ChainResidueDetails
ALEU751-VAL765
ALEU1426-LEU1440

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues138
DetailsTOPO_DOM: Extracellular => ECO:0000250
ChainResidueDetails
AMET1-PHE32
ALEU95-ARG99
ASER154-PHE171
ALEU324-GLY349
ALEU448-PRO450
AVAL555-ASN576
AALA985-LEU1021
ASER1107
ALEU1221-ASN1222

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLN33-LEU53

site_idSWS_FT_FI3
Number of Residues1015
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
ALEU54-LYS73
ALEU121-GLN132
ALYS193-ALA302
ATYR371-PHE426
ALYS472-THR533
ASER598-ALA963
AVAL1043-PRO1085
ATYR1129-VAL1199
AILE1244-ALA1527

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AMET74-GLY94

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AALA100-THR120

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ASER133-ARG153

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATHR172-GLU192

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU303-LEU323

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
APHE350-TYR370

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=8 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALEU427-ASN447

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ASER451-VAL471

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATHR534-TYR554

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AILE577-VAL597

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ALYS964-ALA984

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=13 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLN1022-ARG1042

site_idSWS_FT_FI16
Number of Residues20
DetailsTRANSMEM: Helical; Name=14 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AVAL1086-ALA1106

site_idSWS_FT_FI17
Number of Residues20
DetailsTRANSMEM: Helical; Name=15 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
ATHR1108-PHE1128

site_idSWS_FT_FI18
Number of Residues20
DetailsTRANSMEM: Helical; Name=16 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
AGLU1200-SER1220

site_idSWS_FT_FI19
Number of Residues20
DetailsTRANSMEM: Helical; Name=17 => ECO:0000255|PROSITE-ProRule:PRU00441
ChainResidueDetails
APRO1223-MET1243

site_idSWS_FT_FI20
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY661
AGLY1323

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER908

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER911

site_idSWS_FT_FI23
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN18
AASN1006
AASN1007

227111

PDB entries from 2024-11-06

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