PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15231846-7	2004	On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT.	Serine	123-129	streptothricin acetyltransferase	Escherichia coli	133-136	
15231846-1	2004	Serine acetyltransferase (SAT) catalyzes the first step of cysteine synthesis in microorganisms and higher plants.	Cysteine	59-67	streptothricin acetyltransferase	Escherichia coli	26-29	
15231846-2	2004	Here we present the 2.2 A crystal structure of SAT from Escherichia coli, which is a dimer of trimers, in complex with cysteine.	Cysteine	119-127	streptothricin acetyltransferase	Escherichia coli	47-50	
15231846-5	2004	This structure shows the mechanism by which cysteine inhibits SAT activity and thus controls its own synthesis.	Cysteine	44-52	streptothricin acetyltransferase	Escherichia coli	62-65	
15231846-7	2004	On the basis of the geometry around the cysteine binding site, we are able to suggest a mechanism for the O-acetylation of serine by SAT.	Cysteine	40-48	streptothricin acetyltransferase	Escherichia coli	133-136