PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10480597-5	1999	The glucose is predicted to form hydrogen bond interactions with the side chains of glucokinase residues Thr 168, Lys 169, Asn 204, Asp 205, Asn 231, and Glu 290, similar to those observed for brain hexokinase I.	Glutamic Acid	154-157	glucokinase	Homo sapiens	84-95	
32901087-4	2020	We analyzed glucokinase mutants and identified three glutamate residues that mediate binding to L-arginine.	Glutamic Acid	53-62	glucokinase	Homo sapiens	12-23	
16832733-5	2006	The steady state is switched to the oscillatory state by a first increase of the conductance of the glucokinase-catalyzed reaction at an elevated [Glu] of 10 mM.	Glutamic Acid	147-150	glucokinase	Homo sapiens	100-111	
7961659-8	1994	The results 1) confirm the predictions of the model that Asn-204, Glu-256, and Glu-290 are important residues involved in catalysis and hydrogen bonding glucose hydroxyl groups, 2) provide evidence for a role of Lys-56 in hexose binding, and 3) are consistent with the cooperative behavior of glucokinase being mediated by interactions of other regions of the protein with the highly conserved active site glucose binding residues.	Glutamic Acid	79-82	glucokinase	Homo sapiens	293-304