8SA0: ATP-dependent translocase ABCB1

CryoEM structure of P-Glycoprotein in occluded closed state under continuous turnover conditions with verapamil. Determined by electron microscopy at 4.1 Å resolution. Released 23 Apr 2025.

Method: Electron microscopy
Resolution: 4.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,832
Mol. weight: 142.52 kDa
Ligands: ATP, I6H, MG
Released: 23 Apr 2025

Explore 8SA0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SA0 contains 48 α-helices and 25 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: 48 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	45-83	39
α-helix	108-157	50
α-helix	160-165	6
α-helix	168-187	20
α-helix	189-209	21
α-helix	213-237	25
α-helix	240-259	20
α-helix	261-267	7
α-helix	270-313	44
α-helix	317-319	3
α-helix	328-369	42
β-strand	391-399	9	1
β-strand	410-411	2	1
β-strand	414-418	5	1
β-strand	422-427	6	2
α-helix	433-441	9
β-strand	448-453	6	1
β-strand	456-457	2	1
α-helix	458-467	10
β-strand	472	1	2
β-strand	483	1	3
α-helix	484-491	8
α-helix	498-507	10
α-helix	511-515	5
β-strand	523	1	3
α-helix	526-528	3
α-helix	533-546	14
β-strand	551-555	5	2
α-helix	564-575	12
β-strand	581-585	5	2
α-helix	589-594	6
β-strand	597-602	6	2
β-strand	605-610	6	2
α-helix	612-617	6
α-helix	621-629	9
α-helix	697-700	4
α-helix	704-743	40
α-helix	748-797	50
α-helix	801-804	4
α-helix	807-809	3
α-helix	811-819	9
α-helix	822-826	5
α-helix	827-831	5
α-helix	832-852	21
α-helix	857-873	17
α-helix	879-902	24
α-helix	904-909	6
α-helix	913-965	53
α-helix	971-994	24
α-helix	1001-1013	13
β-strand	1026	1	4
β-strand	1035-1041	7	5
β-strand	1056-1060	5	5
β-strand	1065-1070	6	6
α-helix	1076-1083	8
β-strand	1091-1096	6	5
β-strand	1100	1	5
β-strand	1104	1	4
α-helix	1106-1111	6
β-strand	1113-1116	4	6
α-helix	1127-1134	8
α-helix	1142-1152	11
α-helix	1155-1160	6
α-helix	1164-1166	3
α-helix	1178-1191	14
β-strand	1196-1200	5	6
α-helix	1208-1222	15
β-strand	1226-1230	5	6
α-helix	1234-1239	6
β-strand	1242-1247	6	6
β-strand	1250-1255	6	6
α-helix	1257-1262	6
α-helix	1266-1273	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent translocase ABCB1	A	protein	1274	Homo sapiens	P08183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8SA0_1 ATP-dependent translocase ABCB1 (chains A)
MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAII
HGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSG
IGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS
KINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFT
DKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIG
AAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARG
AAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSG
QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF
ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIA
IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG
FDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRS
SLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAII
NGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKA
GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNI
ANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEA
IENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFG
AYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDS
YSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV
QLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVV
SQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD
EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL
LAQKGIYFSMVSVQ

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
I6H	Dexverapamil	C27 H38 N2 O4	1
MG	Magnesium ion	Mg	2

Primary citation

Cryo-EM of human P-glycoprotein reveals an intermediate occluded conformation during active drug transport. Culbertson, A.T., Liao, M. Nat Commun (2025) 16:3619-3619. DOI 10.1038/s41467-025-58561-4 · 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
6C0V 3.4 Å, Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation
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

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