PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31192586-2	2019	Counterintuitively, crystal structures of CatA and its homologues show a cluster of Glu and Asp residues binding the C-terminal carboxylic acid of the product or inhibitor.	Glutamic Acid	84-87	cathepsin A	Homo sapiens	42-46	
31192586-7	2019	In CatA, E69 and E149 form a Glu pair that is important to catalysis as evidenced by the 56-fold decrease in kcat/Km in the E69Q/E149Q variant.	Glutamic Acid	29-32	cathepsin A	Homo sapiens	3-7