Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BHU

Cryo-EM structure of ATP-bound, outward-facing bovine multidrug resistance protein 1 (MRP1)

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	0046943	molecular_function	carboxylic acid 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
A	1905039	biological_process	carboxylic acid transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue ATP A 1601

Chain	Residue
A	ASN412
A	GLN713
A	HIS827
A	GLU1427
A	ASN1428
A	SER1430
A	GLY1432
A	GLN1433
A	MG1603
A	LYS416
A	TRP653
A	GLY681
A	CYS682
A	GLY683
A	LYS684
A	SER685
A	SER686

site_id	AC2
Number of Residues	18
Details	binding site for residue ATP A 1602

Chain	Residue
A	VAL766
A	ASN767
A	SER769
A	GLY770
A	GLY771
A	GLN772
A	GLU1064
A	TYR1301
A	VAL1308
A	THR1328
A	GLY1329
A	GLY1331
A	LYS1332
A	SER1333
A	SER1334
A	GLN1374
A	HIS1485
A	MG1604

site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 1603

Chain	Residue
A	SER685
A	GLN713
A	ASP792
A	ATP1601

site_id	AC4
Number of Residues	3
Details	binding site for residue MG A 1604

Chain	Residue
A	SER1333
A	GLN1374
A	ATP1602

site_id	AC5
Number of Residues	3
Details	binding site for residue CLR A 1605

Chain	Residue
A	GLY1031
A	MET1034
A	ILE1038

site_id	AC6
Number of Residues	5
Details	binding site for residue CLR A 1606

Chain	Residue
A	MET966
A	PHE1093
A	MET1094
A	ARG1130
A	GLU1254

site_id	AC7
Number of Residues	4
Details	binding site for residue CLR A 1607

Chain	Residue
A	VAL477
A	LEU599
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	120
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	567
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	224
Details	Domain: {"description":"ABC transporter 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	27
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O35379","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P33527","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)