PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28375145-4	2017	Here, the first crystal structure of human 3HAO with the native iron bound in its active site is presented, together with an additional structure with zinc (a known inhibitor of human 3HAO) bound in the active site.	Iron	64-68	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	43-47	
29784877-1	2018	3-Hydroxyanthranilate 3,4-dioxygenase (HAO) is an iron-dependent protein that activates O2 and inserts both oxygen atoms into 3-hydroxyanthranilate (3-HAA).	Iron	50-54	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	0-37	
28375145-2	2017	3HAO is a non-heme iron-containing, ring-cleaving extradiol dioxygenase that catalyzes the addition of both atoms of O2 to the kynurenine pathway metabolite 3-hydroxyanthranilic acid (3-HANA) to form quinolinic acid (QUIN).	Iron	19-23	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	0-4	
21833493-7	2012	In all species, the Fe(2+)-induced increase in 3HAO activity was dose-dependently attenuated by the addition of ferritin, the main iron storage protein in the brain.	Iron	131-135	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	47-51	
25918158-2	2015	A secondary, non-catalytic, rubredoxin-like iron site is conserved in 3-hydroxyanthranilate 3,4-dioxygenase (HAO), from single cellular sources but not multicellular sources.	Iron	44-48	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	70-107	
25588817-1	2015	3-Hydroxyanthranilate 3,4-dioxygenase () is a non-heme iron dependent enzyme.	Iron	55-59	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	0-37	
9870556-1	1998	Iron containing 3-Hydroxyanthranilate oxidase (3HAO) converts 3-hydroxyanthranilate (3HAA) and dioxygen into a precursor which spontaneously converts to quinolinic acid (QA).	Iron	0-4	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	16-45	
16522801-8	2006	Together with two iron-binding residues (His49 and Glu55), Asp120, Asn51, Glu111, and Arg114 form a hydrogen-bonding network; this hydrogen-bond network is key to the catalysis of 3HAO.	Iron	18-22	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	180-184	
9870556-1	1998	Iron containing 3-Hydroxyanthranilate oxidase (3HAO) converts 3-hydroxyanthranilate (3HAA) and dioxygen into a precursor which spontaneously converts to quinolinic acid (QA).	Iron	0-4	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	47-51	
9870556-10	1998	Iron-staining of 3HAO, separated by gel electrophoresis after partial purification by FPLC, showed that loss of iron and loss of enzyme activity during HBO exposure were correlated.	Iron	0-4	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	17-21	
9870556-10	1998	Iron-staining of 3HAO, separated by gel electrophoresis after partial purification by FPLC, showed that loss of iron and loss of enzyme activity during HBO exposure were correlated.	Iron	112-116	3-hydroxyanthranilate 3,4-dioxygenase	Homo sapiens	17-21