Choline Kinase alpha acts through a double-displacement kinetic mechanism involving enzyme isomerisation, as determined through enzyme and inhibitor kinetics and structural biology
The structure was published by Hudson, C.S., Knegtel, R.M., Brown, K., Charlton, P.A., and Pollard, J.R., in 2013 in a paper entitled "Kinetic and mechanistic characterisation of Choline Kinase-alpha." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2012.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Choline kinase alpha.
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 most likely forms homodimers.
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: