PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18186649-10	2008	By comparing the active site residues of the AeKAT-cysteine structure with those of the human KAT I-phenylalanine structure, we determined that Tyr286 in AeKAT is changed to Phe278 in human KAT I, which may explain why AeKAT transaminates hydrophilic amino acids more efficiently than human KAT I does.	Cysteine	51-59	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	47-50	
31408267-4	2019	The seleno-analog Se-TSTD1, in which the active site Cys is replaced with selenocysteine, was also synthesized with a kinetically controlled ligation with an N-to-C synthetic approach.	Cysteine	53-56	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	21-26	
31408267-5	2019	The catalytic activity of the two proteins indicated that Se-TSTD1 possessed only four-fold lower activity than WT-TSTD1, thus suggesting that selenoproteins can have physiologically comparable sulfutransferase activity to their cysteine counterparts.	Cysteine	229-237	thiosulfate sulfurtransferase like domain containing 1	Homo sapiens	61-66