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Structure paper

TitleSubstrate binding and catalytic mechanism of human choline acetyltransferase.
Journal, issue, pagesBiochemistry, Vol. 45, Page 14621-14631, Year 2006
Publish dateFeb 7, 2006 (structure data deposition date)
AuthorsKim, A.R. / Rylett, R.J. / Shilton, B.H.
External linksBiochemistry / PubMed:17144655
MethodsX-ray diffraction
Resolution2.25 - 2.6 Å
Structure data

PDB-2fy2:
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-2fy3:
Structures of ligand bound human choline acetyltransferase provides insight into regulation of acetylcholine synthesis
Method: X-RAY DIFFRACTION / Resolution: 2.27 Å

PDB-2fy4:
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2fy5:
Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CHT:
CHOLINE ION

ChemComp-GOL:
GLYCEROL

ChemComp-COA:
COENZYME A

ChemComp-SOP:
[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / two domain / alpha-beta protein / choline / glycerol / coenzyme A / S-2-(oxopropyl)-coenzyme A

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