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TitleConformational variations of both phosphodiesterase-5 and inhibitors provide the structural basis for the physiological effects of vardenafil and sildenafil.
Journal, issue, pagesMol. Pharmacol., Vol. 73, Page 104-110, Year 2008
Publish dateOct 19, 2007 (structure data deposition date)
AuthorsWang, H. / Ye, M. / Robinson, H. / Francis, S.H. / Ke, H.
External linksMol. Pharmacol. / PubMed:17959709
MethodsX-ray diffraction
Resolution2.07 Å
Structure data

PDB-3b2r:
Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil
Method: X-RAY DIFFRACTION / Resolution: 2.07 Å

Chemicals

ChemComp-VDN:
2-{2-ETHOXY-5-[(4-ETHYLPIPERAZIN-1-YL)SULFONYL]PHENYL}-5-METHYL-7-PROPYLIMIDAZO[5,1-F][1,2,4]TRIAZIN-4(1H)-ONE / medication, inhibitor*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / cGMP phosphodiesterase; PDE5-inhibitor potency; vardenafil; sildenafil; LevitraTM. / Allosteric enzyme / Alternative splicing / cGMP-binding / Magnesium / Metal-binding / Nucleotide-binding / Phosphorylation / Polymorphism / Zinc

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