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Structure paper

TitleHuman butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structure.
Journal, issue, pagesFEBS J., Vol. 279, Page 2905-2916, Year 2012
Publish dateApr 16, 2012 (structure data deposition date)
AuthorsBrazzolotto, X. / Wandhammer, M. / Ronco, C. / Trovaslet, M. / Jean, L. / Lockridge, O. / Renard, P.Y. / Nachon, F.
External linksFEBS J. / PubMed:22726956
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-4aqd:
Crystal structure of fully glycosylated human butyrylcholinesterase
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-BAL:
BETA-ALANINE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-UNX:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-GLY:
GLYCINE

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / ACETYLCHOLINESTERASE / EXPRESSION / HUPRINE / SERINE HYDROLASE / CATALYTIC TRIAD / INSECT CELLS / GLYCOSYLATIONS

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