Identical Ligands in BindingDB

Found 3 hits Enzyme Inhibition Constant Data   

Target/Host (Institution)	Ligand	Target/Host Links	Ligand Links	Trg + Lig Links	Ki nM	ΔG° kJ/mole	IC50 nM	Kd nM	EC50/IC50 nM	koff s-1	kon M-1s-1	pH	Temp °C
cGMP-specific 3',5'-cyclic phosphodiesterase [535-860]   (326/326 = 100%)† (Homo sapiens (Human))	BDBM15338 (5,7-dihydroxy-2-(4-methoxyphenyl)-8-(3-methylbutyl...) Show SMILES COc1ccc(cc1)-c1oc2c(CCC(C)C)c(O)cc(O)c2c(=O)c1O[C@@H]1O[C@@H](C)[C@H](O)[C@@H](O)[C@H]1O |r| Show InChI InChI=1S/C27H32O10/c1-12(2)5-10-16-17(28)11-18(29)19-21(31)26(37-27-23(33)22(32)20(30)13(3)35-27)24(36-25(16)19)14-6-8-15(34-4)9-7-14/h6-9,11-13,20,22-23,27-30,32-33H,5,10H2,1-4H3/t13-,20-,22+,23+,27-/m0/s1	PDB MMDB KEGG UniProtKB/SwissProt B.MOAD DrugBank GoogleScholar AffyNet	KEGG MMDB PC cid PC sid PDB UniChem Similars	MMDB PDB Article PubMed	n/a	n/a	1.70E+3	n/a	n/a	n/a	n/a	7.8	24
University of North Carolina at Chapel Hill					Assay Description Enzymatic activity of the isolated catalytic domains of wild type PDE5A1 and its deletion mutants was assayed by using [3H]cGMP as substrate in a rea...				J Biol Chem 281: 21469-79 (2006) Article DOI: 10.1074/jbc.M512527200 BindingDB Entry DOI: 10.7270/Q290221F
					More data for this Ligand-Target Pair				3D Structure (crystal)
cGMP-specific 3',5'-cyclic phosphodiesterase [1-662,679-875]   (310/326 = 95%)† (Homo sapiens (Human))	BDBM15338 (5,7-dihydroxy-2-(4-methoxyphenyl)-8-(3-methylbutyl...) Show SMILES COc1ccc(cc1)-c1oc2c(CCC(C)C)c(O)cc(O)c2c(=O)c1O[C@@H]1O[C@@H](C)[C@H](O)[C@@H](O)[C@H]1O |r| Show InChI InChI=1S/C27H32O10/c1-12(2)5-10-16-17(28)11-18(29)19-21(31)26(37-27-23(33)22(32)20(30)13(3)35-27)24(36-25(16)19)14-6-8-15(34-4)9-7-14/h6-9,11-13,20,22-23,27-30,32-33H,5,10H2,1-4H3/t13-,20-,22+,23+,27-/m0/s1	PDB UniProtKB/SwissProt GoogleScholar AffyNet	KEGG MMDB PC cid PC sid PDB UniChem Similars	PDB Article PubMed	n/a	n/a	2.50E+3	n/a	n/a	n/a	n/a	7.8	24
University of North Carolina at Chapel Hill					Assay Description Enzymatic activity of the isolated catalytic domains of wild type PDE5A1 and its deletion mutants was assayed by using [3H]cGMP as substrate in a rea...				J Biol Chem 281: 21469-79 (2006) Article DOI: 10.1074/jbc.M512527200 BindingDB Entry DOI: 10.7270/Q290221F
					More data for this Ligand-Target Pair				3D Structure (crystal)
cGMP-specific 3',5'-cyclic phosphodiesterase [1-660,682-875]   (305/326 = 94%)† (Homo sapiens (Human))	BDBM15338 (5,7-dihydroxy-2-(4-methoxyphenyl)-8-(3-methylbutyl...) Show SMILES COc1ccc(cc1)-c1oc2c(CCC(C)C)c(O)cc(O)c2c(=O)c1O[C@@H]1O[C@@H](C)[C@H](O)[C@@H](O)[C@H]1O |r| Show InChI InChI=1S/C27H32O10/c1-12(2)5-10-16-17(28)11-18(29)19-21(31)26(37-27-23(33)22(32)20(30)13(3)35-27)24(36-25(16)19)14-6-8-15(34-4)9-7-14/h6-9,11-13,20,22-23,27-30,32-33H,5,10H2,1-4H3/t13-,20-,22+,23+,27-/m0/s1	PDB UniProtKB/SwissProt GoogleScholar AffyNet	KEGG MMDB PC cid PC sid PDB UniChem Similars	PDB Article PubMed	n/a	n/a	5.50E+4	n/a	n/a	n/a	n/a	7.8	24
University of North Carolina at Chapel Hill					Assay Description Enzymatic activity of the isolated catalytic domains of wild type PDE5A1 and its deletion mutants was assayed by using [3H]cGMP as substrate in a rea...				J Biol Chem 281: 21469-79 (2006) Article DOI: 10.1074/jbc.M512527200 BindingDB Entry DOI: 10.7270/Q290221F
					More data for this Ligand-Target Pair				3D Structure (crystal)

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