6Q81
Structure of P-glycoprotein(ABCB1) in the post-hydrolytic state
Summary for 6Q81
Entry DOI | 10.2210/pdb6q81/pdb |
EMDB information | 4391 |
Descriptor | P-glycoprotein (ABCB1), ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
Functional Keywords | p-glycoprotein; abcb1; atp-binding cassette; transporter; membrane protein; protein structure, membrane protein |
Biological source | Mus musculus |
Total number of polymer chains | 1 |
Total formula weight | 141661.17 |
Authors | Ford, R.C.,Thonghin, N.,Collins, R.F.,Barbieri, A.,Shafi, T.,Siebert, A. (deposition date: 2018-12-13, release date: 2018-12-26, Last modification date: 2024-05-15) |
Primary citation | Thonghin, N.,Collins, R.F.,Barbieri, A.,Shafi, T.,Siebert, A.,Ford, R.C. Novel features in the structure of P-glycoprotein (ABCB1) in the post-hydrolytic state as determined at 7.9 angstrom resolution. Bmc Struct.Biol., 18:17-17, 2018 Cited by PubMed Abstract: P-glycoprotein (ABCB1) is an ATP-binding cassette transporter that plays an important role in the clearance of drugs and xenobiotics and is associated with multi-drug resistance in cancer. Although several P-glycoprotein structures are available, these are either at low resolution, or represent mutated and/or quiescent states of the protein. PubMed: 30545335DOI: 10.1186/s12900-018-0098-z PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (7.9 Å) |
Structure validation
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