PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9275185-7	1997	Interestingly, deletion of amino acids 353-835 in the putative C-terminal regulatory region, or mutation of Lys-35 in the putative ATP-binding domain, markedly reduced the ability of GLK to activate JNK.	Lysine	108-111	glucokinase	Homo sapiens	183-186	
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.	Lysine	212-215	glucokinase	Homo sapiens	293-304	
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.	Lysine	114-117	glucokinase	Homo sapiens	84-95