PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3490371-4	1986	While, for CPA, the half-time of the early phase of the time-activity curve was a function of myocardial oxygen consumption (MVO2), this phase was not found to reflect the oxidative metabolism of IHA.	Oxygen	105-111	carboxypeptidase A1	Homo sapiens	11-14	
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.	Oxygen	370-376	carboxypeptidase A1	Homo sapiens	101-104	
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.	Oxygen	59-65	carboxypeptidase A1	Homo sapiens	151-154	
11937361-6	2002	Inhibitor L- whose stereochemistry belongs to the stereochemical series of substrate binds CPA like substrate does with its carbonyl oxygen coordinating to the active site zinc ion.	Oxygen	133-139	carboxypeptidase A1	Homo sapiens	91-94	
11677137-3	2001	The molecular modeling study for CPA(2R,3R)-3 complex suggested that the lone pair electrons on the nitrogen of the aziridine ring in the inhibitor forms a coordinative bond with the active site zinc ion and the proton on the nitrogen is engaged in hydrogen bonding with one of the carboxylate oxygens of Glu-270.	Oxygen	294-301	carboxypeptidase A1	Homo sapiens	33-36	
15080932-3	2004	(R)-N-Hydroxy-N-sulfamoyl-beta-phenylalanine (8) was shown to be also a potent CPA inhibitor (Ki = 39 microM), the high potency of which may be ascribed to the involvement of the hydroxyl in the binding of CPA, most likely forming bidentate coordinative bonds to the zinc ion in CPA together with the sulfamoyl oxygen atom.	Oxygen	311-317	carboxypeptidase A1	Homo sapiens	79-82