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2FY5

Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis

Summary for 2FY5
Entry DOI10.2210/pdb2fy5/pdb
Related2fy2 2fy3 2fy4
DescriptorCholine 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 Keywordstwo domain, alpha-beta protein, transferase, s-2-(oxopropyl)-coenzyme a
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight68936.95
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 citationKim, 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: 17144655
DOI: 10.1021/bi061536l
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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