6C0V: Multidrug resistance protein 1

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation. Determined by electron microscopy at 3.4 Å resolution. Released 31 Jan 2018.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 8,976
Mol. weight: 143.72 kDa
Ligands: ATP, MG
Released: 31 Jan 2018

Explore 6C0V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6C0V contains 52 α-helices and 29 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 52 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	45-67	23
α-helix	70-78	9
α-helix	106-156	51
α-helix	160-165	6
α-helix	168-170	3
α-helix	171-185	15
α-helix	188-210	23
α-helix	214-219	6
α-helix	222-259	38
α-helix	261-267	7
α-helix	270-318	49
α-helix	320-323	4
α-helix	328-361	34
α-helix	363-370	8
β-strand	383	1	1
β-strand	391-395	5	2
β-strand	398-399	2	3
β-strand	410-411	2	3
β-strand	414-418	5	2
β-strand	422-426	5	4
α-helix	433-440	8
β-strand	448	1	3
β-strand	452-453	2	2
β-strand	456-457	2	2
β-strand	461	1	1
α-helix	463-467	5
β-strand	470-473	4	4
β-strand	483	1	5
α-helix	484-489	6
α-helix	497-507	11
α-helix	511-515	5
β-strand	523	1	5
α-helix	533-547	15
β-strand	551-555	5	4
α-helix	563-575	13
β-strand	581-585	5	4
α-helix	590-593	4
β-strand	597-602	6	4
β-strand	605-610	6	4
α-helix	612-617	6
α-helix	621-629	9
α-helix	697-703	7
α-helix	708-722	15
α-helix	724-739	16
α-helix	748-796	49
α-helix	801-804	4
α-helix	811-829	19
α-helix	831-852	22
α-helix	858-862	5
α-helix	865-902	38
α-helix	904-910	7
α-helix	914-923	10
α-helix	925-966	42
α-helix	971-981	11
α-helix	984-992	9
α-helix	995-1013	19
β-strand	1035-1042	8	6
β-strand	1053-1060	8	6
β-strand	1065-1069	5	7
α-helix	1077-1083	7
β-strand	1091-1096	6	6
β-strand	1100	1	6
α-helix	1106-1112	7
β-strand	1114-1116	3	7
β-strand	1126	1	8
α-helix	1127-1132	6
α-helix	1142-1152	11
α-helix	1155-1160	6
α-helix	1164-1166	3
α-helix	1167	1
β-strand	1168	1	8
α-helix	1169	1
α-helix	1178-1190	13
β-strand	1196-1200	5	7
α-helix	1208-1220	13
β-strand	1226-1230	5	7
α-helix	1234-1239	6
β-strand	1242-1247	6	7
β-strand	1250-1255	6	7
α-helix	1257-1262	6
α-helix	1266-1272	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Multidrug resistance protein 1	A	protein	1289	Homo sapiens	P08183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6C0V_1 Multidrug resistance protein 1 (chains A)
MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAII
HGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSG
IGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS
KINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFT
DKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIG
AAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARG
AAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSG
QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF
ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIA
IARALVRNPKILLLDQATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG
FDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRS
SLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAII
NGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKA
GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNI
ANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEA
IENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFG
AYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDS
YSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV
QLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVV
SQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD
QATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL
LAQKGIYFSMVSVQAGTKRQSNSLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation. Kim, Y., Chen, J. Science (2018) 359:915-919. DOI 10.1126/science.aar7389 · PubMed

Other PDB entries of the same protein (UniProt P08183 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8Y6H 2.49 Å, P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in LMNG detergent
8Y6I 2.54 Å, P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in nanodisc
7A69 3.2 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and vincristine
9CTG 3.4 Å, SapNP Reconstituted Human ABCB1 bound to ATP gammaS
7A6F 3.5 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and zosuquidar
7O9W 3.5 Å, Encequidar-bound human P-glycoprotein in complex with UIC2-Fab
6FN1 3.58 Å, Zosuquidar and UIC2 Fab complex of human-mouse chimeric ABCB1 (ABCB1HM)
6QEX 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with UIC2 fab and taxol
7A6C 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and elacridar
7A6E 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and tariquidar
9CTC 3.6 Å, SapNP reconstituted Human ABCB1 in complex with Zosuquidar and ATP/Mg
9CR8 3.8 Å, SapNP reconstituted human ABCB1

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