Crystal structure of human glucokinase
The structure was published by Kamata, K., Mitsuya, M., Nishimura, T., Eiki, J., and Nagata, Y., in 2004 in a paper entitled "Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2003.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of glucokinase isoform 2. This molecule has the UniProt identifier P35557 (HXK4_HUMAN). The sample contained 455 residues which is 97% of the natural sequence. Out of 455 residues 448 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: