3B2R
Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil
Summary for 3B2R
Entry DOI | 10.2210/pdb3b2r/pdb |
Descriptor | cGMP-specific 3',5'-cyclic phosphodiesterase, 2-{2-ETHOXY-5-[(4-ETHYLPIPERAZIN-1-YL)SULFONYL]PHENYL}-5-METHYL-7-PROPYLIMIDAZO[5,1-F][1,2,4]TRIAZIN-4(1H)-ONE (3 entities in total) |
Functional Keywords | cgmp phosphodiesterase; pde5-inhibitor potency; vardenafil; sildenafil; levitratm., allosteric enzyme, alternative splicing, cgmp-binding, hydrolase, magnesium, metal-binding, nucleotide-binding, phosphorylation, polymorphism, zinc |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 77381.21 |
Authors | Huanchen, W.,Mengchun, Y.,Howard, R.,Sharron, H.F.,Hengming, K. (deposition date: 2007-10-19, release date: 2008-05-20, Last modification date: 2024-04-03) |
Primary citation | Wang, H.,Ye, M.,Robinson, H.,Francis, S.H.,Ke, H. Conformational variations of both phosphodiesterase-5 and inhibitors provide the structural basis for the physiological effects of vardenafil and sildenafil. Mol.Pharmacol., 73:104-110, 2008 Cited by PubMed: 17959709DOI: 10.1124/mol.107.040212 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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