2fy5 Summary

pdbe.org/2fy5
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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 2.6 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 577 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 94%


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