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). 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):
This entry contains 1 unique UniProt protein: