2fy4 Summary


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

The structure was published by Kim, A.R., Rylett, R.J., and Shilton, B.H., in 2006 in a paper entitled "Substrate binding and catalytic mechanism of human choline acetyltransferase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2006.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Choline O-acetyltransferase. This molecule has the UniProt identifier P28329 (CLAT_HUMAN)search. The sample contained 612 residues which is < 90% of the natural sequence. Out of 612 residues 589 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Choline O-acetyltransferase P28329 (120-733) (CLAT_HUMAN)search Homo sapienssearch < 90% 612 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P28329 (120 - 733) Choline O-acetyltransferase Homo sapiens

Chain Sequence family (Pfam)
A Choline/Carnitine o-acyltransferasesearch

Chain ID Molecular function (GO)
A (P28329) transferase activity, transferring acyl groupssearch

Chain InterPro annotation
A Acyltransferase ChoActase/COT/CPTsearch