Catalytic complex of Human Glucokinase
The structure was published by Petit, P., Antoine, M., Ferry, G., et al., Gluais, L., Vincentelli, R., and Vuillard, L., in 2011 in a paper entitled "The active conformation of human glucokinase is not altered by allosteric activators" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Glucokinase. This molecule has the UniProt identifier P35557 (HXK4_HUMAN). The sample contained 470 residues which is 98% of the natural sequence. Out of 470 residues 447 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: