9CTF: SapNP Reconstituted Human ABCB1

SapNP Reconstituted Human ABCB1 bound to Taxol in presence of ATP. Determined by electron microscopy at 3.9 Å resolution. Released 22 Jan 2025.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 9,398
Mol. weight: 153.54 kDa
Ligands: UPL, ATP, TA1
Released: 22 Jan 2025

Explore 9CTF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CTF contains 48 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: 48 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	35-39	5
α-helix	46-86	41
α-helix	101-157	57
α-helix	160-164	5
α-helix	168-186	19
α-helix	188-208	21
α-helix	212-257	46
α-helix	261-267	7
α-helix	270-322	53
α-helix	328-346	19
α-helix	349-370	22
β-strand	383	1	1
β-strand	392-398	7	2
α-helix	402-404	3
β-strand	413-417	5	2
β-strand	422-426	5	3
α-helix	433-440	8
β-strand	448-453	6	2
β-strand	456-457	2	2
β-strand	461	1	1
α-helix	463-469	7
β-strand	470-473	4	3
β-strand	483	1	4
α-helix	484-489	6
α-helix	497-506	10
α-helix	510-514	5
α-helix	519-521	3
β-strand	523	1	4
α-helix	533-546	14
β-strand	551-555	5	3
α-helix	563-576	14
β-strand	581-585	5	3
α-helix	591-594	4
β-strand	597-600	4	3
β-strand	602	1	5
β-strand	605	1	5
β-strand	609-610	2	3
α-helix	612-618	7
α-helix	621-629	9
α-helix	696-702	7
α-helix	708-722	15
α-helix	724-738	15
α-helix	745-798	54
α-helix	801-805	5
α-helix	811-816	6
α-helix	817-821	5
α-helix	822-827	6
α-helix	831-853	23
α-helix	855-901	47
α-helix	904-909	6
α-helix	913-965	53
α-helix	971-994	24
α-helix	999-1013	15
β-strand	1026	1	6
β-strand	1036-1039	4	7
β-strand	1040-1042	3	8
β-strand	1053-1056	4	8
β-strand	1059	1	7
β-strand	1066-1069	4	9
α-helix	1076-1083	8
β-strand	1091-1096	6	7
β-strand	1099-1100	2	7
α-helix	1101-1103	3
β-strand	1104	1	6
α-helix	1106-1110	5
β-strand	1113-1116	4	9
β-strand	1125-1126	2	10
α-helix	1127-1132	6
α-helix	1142-1152	11
α-helix	1155-1158	4
α-helix	1164-1166	3
β-strand	1168-1169	2	10
β-strand	1174	1	10
α-helix	1178-1191	14
β-strand	1196-1199	4	9
α-helix	1202-1204	3
α-helix	1208-1222	15
β-strand	1226-1229	4	9
α-helix	1235-1237	3
β-strand	1242-1247	6	9
β-strand	1250-1256	7	9

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

>9CTF_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
UPL	Unknown branched fragment of phospholipid	C34 H70	22
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
TA1	Taxol	C47 H51 N O14	1

Primary citation

Structural insights into binding-site access and ligand recognition by human ABCB1. Kurre, D., Dang, P.X., Le, L.T.M. et al. EMBO J (2025) 44:991-1006. DOI 10.1038/s44318-025-00361-z · 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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