PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20853826-7	2010	For the GSTP1-1 enzyme, we have demonstrated that a water molecule, after an initial conformational rearrangement of GSH, can assist a proton transfer between the GSH cysteine thiol (GSH-SH) and the GSH glutamate alpha carboxylate (GSH-COO(-)) groups.	Water	52-57	glutathione S-transferase pi 1	Homo sapiens	8-15	
9299520-6	1997	It is proposed that amino acid 113 functions as part of a clamp that lines the mouth of the water channel leading to the active sites of the hGSTP1-1 dimer and controls the access to substrates.	Water	92-97	glutathione S-transferase pi 1	Homo sapiens	141-147	
17587159-4	2007	Moreover, on SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions, hexahistidine-tagged hGST P1-1 (His(6)-hGST P1-1) treated with 1 mM H(2)O(2) showed at least three extra bands, in addition to the native His(6)-hGST P1-1 subunit band.	Water	161-166	glutathione S-transferase pi 1	Homo sapiens	114-123	
15231573-6	2005	Forced expression of GSTP1 by transfection of Raji cells significantly decreased the basal amount of H(2)O(2) and its levels after therapeutic concentration of As(2)O(3) treatment.	Water	101-106	glutathione S-transferase pi 1	Homo sapiens	21-26	
14676193-9	2004	A network of hydrogen-bonded water molecules, found in crystal structures of GSTP1-1, connects the two active sites and the main chain carbonyl group of Tyr(50), thereby offering a mechanism for communication between the two active sites.	Water	29-34	glutathione S-transferase pi 1	Homo sapiens	77-84	
9882456-0	1999	Quantitative differences in the active-site hydrophobicity of five human glutathione S-transferase isoenzymes: water-soluble carcinogen-selective properties of the neoplastic GSTP1-1 species.	Water	111-116	glutathione S-transferase pi 1	Homo sapiens	175-182	
12718659-2	2001	However, the species of glutathione S-transferases (GSTP1-1) linked to neoplasia of rat and human were recently shown to be selective for hydrophilic carcinogens such as acrolein and hydroxyalkenals (Satoh, 1998; Satoh et al., 1999) in accord with the finding of a water-network in the active site of the human GSTP1-1 by X-ray analysis (Hu et al.	Water	265-270	glutathione S-transferase pi 1	Homo sapiens	311-318	
32473836-0	2020	Characterization of water-soluble esters of nitrobenzoxadiazole-based GSTP1-1 inhibitors for cancer treatment.	Water	20-25	glutathione S-transferase pi 1	Homo sapiens	70-77	
25606397-1	2014	Glutathione S-transferases (GSTs) belong to a super family of phase II detoxification enzymes, which play an important role in protecting cells from damage caused by endogenous and exogenous compounds by conjugating reactive intermediates with glutathione to produce less reactive water-soluble compounds.	Water	281-286	glutathione S-transferase pi 1	Homo sapiens	28-32	
9245401-4	1997	In hGSTP1-1, the cavity is approximately half hydrophobic and half hydrophilic and is defined by the side chains of Y7, F8, V10, R13, V104, Y108, N204, and G205 and five water molecules.	Water	170-175	glutathione S-transferase pi 1	Homo sapiens	3-11