PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7756988-0	1994	The structures of RNase A complexed with 3"-CMP and d(CpA): active site conformation and conserved water molecules.	Water	99-104	carboxypeptidase A1	Homo sapiens	54-57	
11093266-9	2001	In the case of one of the substrates, CpA, we have also identified the presence of a water molecule that invariantly bridges the B2 base with the protein.	Water	85-90	carboxypeptidase A1	Homo sapiens	38-41	
9801832-2	1998	The crystal structure reveals that both the amide carbonyl oxygen and the terminal amino nitrogen of Gly-Tyr coordinate to the active site zinc ion of CPA in a bidentate fashion, whereby the zinc-bound water molecule is displaced by the amino group.	Water	202-207	carboxypeptidase A1	Homo sapiens	151-154	
9801832-3	1998	As to the catalytic mechanism of CPA, it is generally believed that while in the cases of ester substrates the carboxylate of Glu-270 functions as the nucleophile which attacks the scissile carbonyl carbon (anhydride pathway), in the case of peptide substrates the zinc-bound water molecule attacks the scissile peptide bond (general base pathway).	Water	276-281	carboxypeptidase A1	Homo sapiens	33-36	
3422451-7	1988	The structure of the CPA-hydrated BBP complex provides support for a promoted-water hydrolytic mechanism, although it is not certain whether the enzyme has actually participated in the hydration reaction at the ketone carbonyl of BBP.	Water	78-83	carboxypeptidase A1	Homo sapiens	21-24	
2026592-7	1991	A solvent deuterium isotope effect of 1.39 +/- 0.02 was noted for inactivation by 2 and one of 1.31 +/- 0.01 for its hydrolysis, in keeping with a proposed promoted water hydrolytic pathway for peptide hydrolysis by CPA (Christanson, D. W., and Lipscomb, W. N. (1989) Acc.	Water	165-170	carboxypeptidase A1	Homo sapiens	216-219	
24649826-8	2014	RESULTS: For equilibration with CPA, our algorithm predicts an optimal first step consisting of exposure to a solution containing only water and CPA.	Water	135-140	carboxypeptidase A1	Homo sapiens	32-35	
23526979-5	2013	Simulation results suggest that cell nuclear plays a significant role in cryo-dehydration and would affect water/CPA concentration gradient inside the cell.	Water	107-112	carboxypeptidase A1	Homo sapiens	113-116	
20141508-5	2006	This is achieved either by directly coordinating to the metal ion found in some metalloenzymes (CAs, CPA, STS), usually by means of one of the nitrogen atoms present in the sulfamide motif, or, as in the case of the cyclic sulfamides, acting as HIV protease inhibitors interacting with the catalytically critical aspartic acid residues of the active site by means of an oxygen atom belonging to the HN-SO(2)-NH motif that substitutes a catalytically essential water molecule.	Water	460-465	carboxypeptidase A1	Homo sapiens	101-104	
32864834-4	2020	Meanwhile, the water solubility of CP-beta-CD is improved dramatically to 816 mg mL-1 , which is 440 times as that of unmodified beta-CD.	Water	15-20	carboxypeptidase A1	Homo sapiens	35-42	
32864834-8	2020	This work suggests that the water soluble CP-beta-CD with excellent cell internalization efficiency has a potential application prospect in the field of drug delivery.	Water	28-33	carboxypeptidase A1	Homo sapiens	42-49