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: 17959709 DOI: 10.1124/mol.107.040212 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.07 Å)

Structure validation