CryoEM structure of P-Glycoprotein in inward facing 1 state under continuous turnover conditions with vinblastine. Determined by electron microscopy at 4.1 Å resolution. Released 23 Apr 2025.
Explore 8SB9 in 3D Show helices and sheets RCSB PDB PDBe
8SB9 contains 53 α-helices and 27 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 | 45-47 | 3 | |
| α-helix | 48-84 | 37 | |
| α-helix | 108-157 | 50 | |
| α-helix | 160-165 | 6 | |
| α-helix | 168-184 | 17 | |
| α-helix | 188-210 | 23 | |
| α-helix | 214-259 | 46 | |
| α-helix | 261-267 | 7 | |
| α-helix | 270-322 | 53 | |
| α-helix | 328-347 | 20 | |
| α-helix | 349-370 | 22 | |
| β-strand | 383 | 1 | 1 |
| β-strand | 392-399 | 8 | 2 |
| α-helix | 402-404 | 3 | |
| β-strand | 410-411 | 2 | 2 |
| β-strand | 415-417 | 3 | 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 | 463-468 | 6 | |
| β-strand | 470-473 | 4 | 3 |
| α-helix | 484-489 | 6 | |
| α-helix | 497-507 | 11 | |
| α-helix | 510-515 | 6 | |
| α-helix | 533-546 | 14 | |
| β-strand | 551-555 | 5 | 3 |
| α-helix | 563-577 | 15 | |
| β-strand | 581-585 | 5 | 3 |
| α-helix | 589-593 | 5 | |
| β-strand | 597-602 | 6 | 3 |
| β-strand | 605-610 | 6 | 3 |
| α-helix | 612-617 | 6 | |
| α-helix | 621-629 | 9 | |
| α-helix | 702-706 | 5 | |
| α-helix | 708-740 | 33 | |
| α-helix | 747-797 | 51 | |
| α-helix | 801-805 | 5 | |
| 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 | 856-878 | 23 | |
| α-helix | 886-893 | 8 | |
| α-helix | 895-902 | 8 | |
| α-helix | 904-909 | 6 | |
| α-helix | 913-965 | 53 | |
| α-helix | 971-994 | 24 | |
| α-helix | 996-997 | 2 | |
| α-helix | 998-1013 | 16 | |
| β-strand | 1026 | 1 | 4 |
| β-strand | 1035-1041 | 7 | 5 |
| β-strand | 1056-1060 | 5 | 5 |
| β-strand | 1065-1069 | 5 | 6 |
| α-helix | 1076-1083 | 8 | |
| β-strand | 1091-1096 | 6 | 5 |
| β-strand | 1100 | 1 | 5 |
| β-strand | 1104 | 1 | 4 |
| α-helix | 1106-1112 | 7 | |
| β-strand | 1114-1116 | 3 | 6 |
| β-strand | 1126 | 1 | 7 |
| α-helix | 1127-1132 | 6 | |
| α-helix | 1139-1141 | 3 | |
| α-helix | 1142-1152 | 11 | |
| α-helix | 1155-1160 | 6 | |
| α-helix | 1164-1166 | 3 | |
| α-helix | 1167 | 1 | |
| β-strand | 1168 | 1 | 7 |
| α-helix | 1169-1170 | 2 | |
| α-helix | 1178-1191 | 14 | |
| β-strand | 1196-1200 | 5 | 6 |
| α-helix | 1208-1222 | 15 | |
| β-strand | 1226-1230 | 5 | 6 |
| α-helix | 1235-1238 | 4 | |
| β-strand | 1242-1247 | 6 | 6 |
| β-strand | 1250-1255 | 6 | 6 |
| α-helix | 1257-1262 | 6 | |
| α-helix | 1266-1274 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ATP-dependent translocase ABCB1 | A | protein | 1280 | Homo sapiens | P08183 (AlphaFold model) |
>8SB9_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 | 2 |
| MG | Magnesium ion | Mg | 2 |
| VLB | (2ALPHA,2'BETA,3BETA,4ALPHA,5BETA)-vincaleukoblastine | C46 H58 N4 O9 | 2 |
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:
MolViewer shows 8SB9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.