8SB8: ATP-dependent translocase ABCB1

CryoEM structure of P-Glycoprotein in collapsed closed state with vanadate. Determined by electron microscopy at 3.9 Å resolution. Released 23 Apr 2025.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 7,340
Mol. weight: 142.78 kDa
Ligands: AOV, MG
Released: 23 Apr 2025

Explore 8SB8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8SB8 contains 47 α-helices and 33 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: 47 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	38-40	3
α-helix	45-75	31
α-helix	107-157	51
α-helix	160-165	6
α-helix	169-210	42
α-helix	213-259	47
α-helix	261-267	7
α-helix	270-323	54
α-helix	328-369	42
β-strand	383	1	1
β-strand	392-393	2	2
β-strand	397-399	3	3
α-helix	402-404	3
β-strand	410-413	4	3
β-strand	416-417	2	2
β-strand	423-427	5	4
α-helix	433-440	8
β-strand	448	1	3
β-strand	452-453	2	2
β-strand	457	1	2
β-strand	461	1	1
α-helix	463-469	7
β-strand	470-471	2	5
β-strand	483	1	6
α-helix	484-489	6
α-helix	497-506	10
α-helix	510-515	6
α-helix	522	1
β-strand	523	1	6
α-helix	524	1
α-helix	526-528	3
α-helix	533-546	14
β-strand	551-552	2	5
β-strand	555	1	4
α-helix	563-577	15
β-strand	585	1	4
α-helix	589-592	4
β-strand	597-602	6	4
β-strand	605-606	2	4
α-helix	612-618	7
α-helix	621-629	9
α-helix	699-703	5
α-helix	708-724	17
α-helix	727-741	15
α-helix	745-798	54
α-helix	801-805	5
α-helix	811-829	19
α-helix	831-853	23
α-helix	858-902	45
α-helix	904-910	7
α-helix	913-965	53
α-helix	971-987	17
α-helix	989-1013	25
β-strand	1026	1	7
β-strand	1035-1041	7	8
β-strand	1056-1060	5	8
β-strand	1065-1070	6	9
α-helix	1076-1083	8
β-strand	1091-1094	4	8
β-strand	1095-1096	2	10
β-strand	1099-1100	2	10
β-strand	1104	1	7
α-helix	1106-1112	7
β-strand	1113-1115	3	9
β-strand	1126	1	11
α-helix	1127-1132	6
α-helix	1142-1151	10
α-helix	1155-1160	6
α-helix	1164-1166	3
β-strand	1168	1	11
α-helix	1171-1173	3
α-helix	1178-1191	14
β-strand	1196-1200	5	9
α-helix	1208-1220	13
β-strand	1226-1230	5	9
α-helix	1234-1237	4
β-strand	1242-1247	6	9
β-strand	1250-1255	6	9
α-helix	1257-1262	6
α-helix	1266-1272	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent translocase ABCB1	A	protein	1280	Homo sapiens	P08183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8SB8_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
LAQKGIYFSMVSVQAGTKRQ

Ligands and cofactors

ID	Name	Formula	Copies
AOV	ADP orthovanadate	C10 H17 N5 O14 P2 V	2
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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