PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22437839-3	2012	These enzymes share high sequence identity and catalyze 4-pro-(R)-hydride transfer from NADPH to an electrophilic carbon but differ in that one residue in the conserved AKR catalytic tetrad, His(120) (AKR1D1 numbering), is substituted by a glutamate in AKR1D1.	NADP	88-93	aldo-keto reductase family 1 member D1	Homo sapiens	201-207	
7508385-1	1994	The enzyme delta 4-3-oxosteroid 5 beta-reductase (3-oxo-5 beta-steroid: NADP+ oxidoreductase and 4,5 beta-dihydrocortisone: NADP+ delta 4-oxidoreductase) catalyzes the reduction of the delta 4 double bond of bile acid intermediates and steroid hormones carrying the delta 4-3-one structure in the A/B cis configuration.	NADP	72-76	aldo-keto reductase family 1 member D1	Homo sapiens	11-48	
22437839-3	2012	These enzymes share high sequence identity and catalyze 4-pro-(R)-hydride transfer from NADPH to an electrophilic carbon but differ in that one residue in the conserved AKR catalytic tetrad, His(120) (AKR1D1 numbering), is substituted by a glutamate in AKR1D1.	NADP	88-93	aldo-keto reductase family 1 member D1	Homo sapiens	253-259	
18407998-4	2008	We have determined the structures of AKR1D1 complexes with NADP(+) at 1.79- and 1.35-A resolution (HEPES bound in the active site), NADP(+) and cortisone at 1.90-A resolution, NADP(+) and progesterone at 2.03-A resolution, and NADP(+) and testosterone at 1.62-A resolution.	NADP	132-136	aldo-keto reductase family 1 member D1	Homo sapiens	37-43	
19515843-7	2009	The structure of the AKR1D1.NADP(+)*finasteride complex determined at 1.7 A resolution shows that it is not possible for NADPH to reduce the Delta(1-2)-ene of finasteride because the cofactor and steroid are not proximal to each other.	NADP	28-32	aldo-keto reductase family 1 member D1	Homo sapiens	21-27	
19515843-7	2009	The structure of the AKR1D1.NADP(+)*finasteride complex determined at 1.7 A resolution shows that it is not possible for NADPH to reduce the Delta(1-2)-ene of finasteride because the cofactor and steroid are not proximal to each other.	NADP	121-126	aldo-keto reductase family 1 member D1	Homo sapiens	21-27	
19013211-1	2009	Two members of the human aldo-keto reductase (AKR) superfamily participate in the biosynthesis of bile acids by catalyzing the NADP(H) dependent reduction of 3-keto groups (AKR1C4) and Delta4 double bonds (AKR1D1) of oxysterol precursors.	NADP	127-134	aldo-keto reductase family 1 member D1	Homo sapiens	206-212	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-84	aldo-keto reductase family 1 member D1	Homo sapiens	73-79	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-84	aldo-keto reductase family 1 member D1	Homo sapiens	73-79	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-84	aldo-keto reductase family 1 member D1	Homo sapiens	73-79	
18407998-4	2008	We have determined the structures of AKR1D1 complexes with NADP(+) at 1.79- and 1.35-A resolution (HEPES bound in the active site), NADP(+) and cortisone at 1.90-A resolution, NADP(+) and progesterone at 2.03-A resolution, and NADP(+) and testosterone at 1.62-A resolution.	NADP	59-63	aldo-keto reductase family 1 member D1	Homo sapiens	37-43	
18407998-4	2008	We have determined the structures of AKR1D1 complexes with NADP(+) at 1.79- and 1.35-A resolution (HEPES bound in the active site), NADP(+) and cortisone at 1.90-A resolution, NADP(+) and progesterone at 2.03-A resolution, and NADP(+) and testosterone at 1.62-A resolution.	NADP	132-136	aldo-keto reductase family 1 member D1	Homo sapiens	37-43	
18407998-4	2008	We have determined the structures of AKR1D1 complexes with NADP(+) at 1.79- and 1.35-A resolution (HEPES bound in the active site), NADP(+) and cortisone at 1.90-A resolution, NADP(+) and progesterone at 2.03-A resolution, and NADP(+) and testosterone at 1.62-A resolution.	NADP	132-136	aldo-keto reductase family 1 member D1	Homo sapiens	37-43	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	45-49	aldo-keto reductase family 1 member D1	Homo sapiens	38-44	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-88	aldo-keto reductase family 1 member D1	Homo sapiens	73-79	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-88	aldo-keto reductase family 1 member D1	Homo sapiens	73-79	
18848863-2	2009	We have reported the structures of an AKR1D1-NADP(+) binary complex, and AKR1D1-NADP(+)-cortisone, AKR1D1-NADP(+)-progesterone and AKR1D1-NADP(+)-testosterone ternary complexes at high resolutions.	NADP	80-88	aldo-keto reductase family 1 member D1	Homo sapiens	73-79