PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16789430-3	2006	Berberine was found to readily fit within the binding pocket of h-PTP 1B in a low energy orientation characterized with optimal electrostatic attractive interactions bridging the isoquinolinium positively charged nitrogen atom of berberine and the negatively charged acidic residue of ASP 48 of h-PTP 1B.	Aspartic Acid	285-288	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	66-72	
11352902-9	2001	These results suggest that Arg(49) and Asp(50) may be targeted for the design of potent and selective inhibitors of TCPTP and PTP1B.	Aspartic Acid	39-42	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	126-131	
12547827-7	2003	Our data further suggest that potent, yet highly selective, PTP1B inhibitory agents can be acquired by targeting the area defined by residues Lys-41, Arg-47, and Asp-48, in addition to the previously identified second aryl phosphate-binding pocket.	Aspartic Acid	162-165	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	60-65	
10702277-7	2000	In addition, binding of OBA to the active site of PTP1B creates a unique arrangement involving Asp(181), Lys(120), and Tyr(46).	Aspartic Acid	95-98	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	50-55	
9050838-3	1997	From a mutagenesis study of these invariant residues that was guided by our knowledge of the crystal structure of PTP1B, we have discovered a mutation of the invariant catalytic acid (Asp-181 in PTP1B) that converts an extremely active enzyme into a "substrate trap."	Aspartic Acid	184-187	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	114-119	
9050838-3	1997	From a mutagenesis study of these invariant residues that was guided by our knowledge of the crystal structure of PTP1B, we have discovered a mutation of the invariant catalytic acid (Asp-181 in PTP1B) that converts an extremely active enzyme into a "substrate trap."	Aspartic Acid	184-187	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	195-200	
28540523-5	2017	In contrast to zinc, which binds to the phosphocysteine intermediate in the closed conformation of protein tyrosine phosphatase 1B when the catalytic aspartate has moved into the active site, other divalent cations such as cadmium and copper may also bind to the enzyme in the open conformation.	Aspartic Acid	150-159	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	99-130	
22045810-3	2011	Here, we demonstrate that knockdown of PTP1B or expression of a PTP1B trapping aspartic acid-to-alanine substitution (D/A) mutant delayed ligand-induced degradation of the Met and EGF RTKs.	Aspartic Acid	79-92	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	64-69