6I2T
CryoEM reconstruction of full-length, fully-glycosylated human butyrylcholinesterase tetramer
Summary for 6I2T
| Entry DOI | 10.2210/pdb6i2t/pdb |
| EMDB information | 4400 |
| Descriptor | Cholinesterase, lamellipodin-derived polyproline peptide, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | cholinesterase, tetramer, hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 263551.06 |
| Authors | Leung, M.R.,van Bezouwen, L.S.,Schopfer, L.M.,Sussman, J.L.,Silman, I.,Lockridge, O.,Zeev-Ben-Mordehai, T. (deposition date: 2018-11-01, release date: 2018-12-19, Last modification date: 2020-07-29) |
| Primary citation | Leung, M.R.,van Bezouwen, L.S.,Schopfer, L.M.,Sussman, J.L.,Silman, I.,Lockridge, O.,Zeev-Ben-Mordehai, T. Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly. Proc. Natl. Acad. Sci. U.S.A., 115:13270-13275, 2018 Cited by PubMed: 30538207DOI: 10.1073/pnas.1817009115 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.7 Å) |
Structure validation
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