1GC5

CRYSTAL STRUCTURE OF A NOVEL ADP-DEPENDENT GLUCOKINASE FROM THERMOCOCCUS LITORALIS

Summary for 1GC5

Entry DOI	10.2210/pdb1gc5/pdb
Descriptor	ADP-DEPENDENT GLUCOKINASE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywords	alfa/beta sandwichs, induced-fitting, transferase
Biological source	Thermococcus litoralis
Cellular location	Cytoplasm (By similarity): Q7M537
Total number of polymer chains	1
Total formula weight	54045.29
Authors	Ito, S.,Fushinobu, S.,Yoshioka, I.,Koga, S.,Matsuzawa, H.,Wakagi, T. (deposition date: 2000-07-20, release date: 2001-07-25, Last modification date: 2023-12-27)
Primary citation	Ito, S.,Fushinobu, S.,Yoshioka, I.,Koga, S.,Matsuzawa, H.,Wakagi, T. Structural Basis for the ADP-Specificity of a Novel Glucokinase from a Hyperthermophilic Archaeon Structure, 9:205-214, 2001 Cited by PubMed Abstract: ATP is the most common phosphoryl group donor for kinases. However, certain hyperthermophilic archaea such as Thermococcus litoralis and Pyrococcus furiosus utilize unusual ADP-dependent glucokinases and phosphofructokinases in their glycolytic pathways. These ADP-dependent kinases are homologous to each other but show no sequence similarity to any of the hitherto known ATP-dependent enzymes. PubMed: 11286887 DOI: 10.1016/S0969-2126(01)00577-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation