SapNP reconstituted Human ABCB1 in complex with Zosuquidar and ATP/Mg. Determined by electron microscopy at 3.6 Å resolution. Released 22 Jan 2025.
Explore 9CTC in 3D Show helices and sheets RCSB PDB PDBe
9CTC contains 62 α-helices and 21 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-39 | 4 | |
| α-helix | 45-61 | 17 | |
| α-helix | 65-89 | 25 | |
| α-helix | 110-157 | 48 | |
| α-helix | 159 | 1 | |
| α-helix | 162-165 | 4 | |
| α-helix | 168-173 | 6 | |
| α-helix | 174-178 | 5 | |
| α-helix | 179-185 | 7 | |
| α-helix | 188-210 | 23 | |
| α-helix | 212-220 | 9 | |
| α-helix | 222-237 | 16 | |
| α-helix | 248-259 | 12 | |
| α-helix | 261-267 | 7 | |
| α-helix | 270-323 | 54 | |
| α-helix | 328-344 | 17 | |
| α-helix | 349-369 | 21 | |
| β-strand | 392-398 | 7 | 1 |
| α-helix | 402-404 | 3 | |
| β-strand | 413-415 | 3 | 1 |
| β-strand | 422-426 | 5 | 2 |
| α-helix | 435-440 | 6 | |
| β-strand | 448-453 | 6 | 1 |
| β-strand | 457 | 1 | 1 |
| α-helix | 463-469 | 7 | |
| β-strand | 470-473 | 4 | 2 |
| α-helix | 484-491 | 8 | |
| α-helix | 497-506 | 10 | |
| α-helix | 512-515 | 4 | |
| α-helix | 519-521 | 3 | |
| α-helix | 522-524 | 3 | |
| α-helix | 533-546 | 14 | |
| β-strand | 551-555 | 5 | 2 |
| α-helix | 564-576 | 13 | |
| β-strand | 582-585 | 4 | 2 |
| α-helix | 591-593 | 3 | |
| β-strand | 597-600 | 4 | 2 |
| α-helix | 612-618 | 7 | |
| α-helix | 621-629 | 9 | |
| α-helix | 692-696 | 5 | |
| α-helix | 697-703 | 7 | |
| α-helix | 705-707 | 3 | |
| α-helix | 708-722 | 15 | |
| α-helix | 725-740 | 16 | |
| α-helix | 745-798 | 54 | |
| α-helix | 801-805 | 5 | |
| α-helix | 811-816 | 6 | |
| α-helix | 817-821 | 5 | |
| α-helix | 822-824 | 3 | |
| α-helix | 825-828 | 4 | |
| α-helix | 830-839 | 10 | |
| α-helix | 840-844 | 5 | |
| α-helix | 845-853 | 9 | |
| α-helix | 856-861 | 6 | |
| α-helix | 865-879 | 15 | |
| α-helix | 891-901 | 11 | |
| α-helix | 904-909 | 6 | |
| α-helix | 914-965 | 52 | |
| α-helix | 971-981 | 11 | |
| α-helix | 983-991 | 9 | |
| α-helix | 998-1012 | 15 | |
| β-strand | 1035-1041 | 7 | 3 |
| β-strand | 1056-1059 | 4 | 3 |
| β-strand | 1066-1069 | 4 | 4 |
| α-helix | 1075-1083 | 9 | |
| β-strand | 1091-1096 | 6 | 3 |
| β-strand | 1099-1100 | 2 | 3 |
| α-helix | 1106-1111 | 6 | |
| β-strand | 1114-1116 | 3 | 4 |
| β-strand | 1126 | 1 | 5 |
| α-helix | 1127-1131 | 5 | |
| α-helix | 1139-1141 | 3 | |
| α-helix | 1142-1151 | 10 | |
| β-strand | 1168 | 1 | 5 |
| α-helix | 1179-1190 | 12 | |
| β-strand | 1197-1199 | 3 | 4 |
| α-helix | 1210-1222 | 13 | |
| β-strand | 1228-1229 | 2 | 4 |
| α-helix | 1233-1235 | 3 | |
| β-strand | 1242-1247 | 6 | 4 |
| β-strand | 1250-1256 | 7 | 4 |
| α-helix | 1257-1262 | 6 | |
| α-helix | 1266-1269 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ATP-dependent translocase ABCB1 | A | protein | 1280 | Homo sapiens | P08183 (AlphaFold model) |
>9CTC_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
| ID | Name | Formula | Copies |
|---|---|---|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| ZQU | Zosuquidar | C32 H31 F2 N3 O2 | 2 |
| UPL | Unknown branched fragment of phospholipid | C34 H70 | 22 |
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:
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