2FY5
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Summary for 2FY5
Entry DOI | 10.2210/pdb2fy5/pdb |
Related | 2fy2 2fy3 2fy4 |
Descriptor | Choline O-acetyltransferase, [(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL (3R)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-{[3-OXO-3-({2-[(2-OXOPROPYL)THIO]ETHYL}AMINO)PROPYL]AMINO}BUTYL DIHYDROGEN DIPHOSPHATE (3 entities in total) |
Functional Keywords | two domain, alpha-beta protein, transferase, s-2-(oxopropyl)-coenzyme a |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 68936.95 |
Authors | Kim, A.R.,Rylett, R.J.,Shilton, B.H. (deposition date: 2006-02-07, release date: 2006-12-12, Last modification date: 2023-08-30) |
Primary citation | Kim, A.R.,Rylett, R.J.,Shilton, B.H. Substrate binding and catalytic mechanism of human choline acetyltransferase. Biochemistry, 45:14621-14631, 2006 Cited by PubMed: 17144655DOI: 10.1021/bi061536l PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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