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3b2r
From Proteopedia
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==Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil== | ==Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil== | ||
| - | <StructureSection load='3b2r' size='340' side='right' caption='[[3b2r]], [[Resolution|resolution]] 2.07Å' scene=''> | + | <StructureSection load='3b2r' size='340' side='right'caption='[[3b2r]], [[Resolution|resolution]] 2.07Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3b2r]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3b2r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B2R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=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'>VDN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=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'>VDN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE5A, PDE5 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE5A, PDE5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3',5'-cyclic-GMP_phosphodiesterase 3',5'-cyclic-GMP phosphodiesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.35 3.1.4.35] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b2r OCA], [https://pdbe.org/3b2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b2r RCSB], [https://www.ebi.ac.uk/pdbsum/3b2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b2r ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PDE5A_HUMAN PDE5A_HUMAN]] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
| - | *[[Phosphodiesterase|Phosphodiesterase]] | + | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 39: | Line 39: | ||
[[Category: 3',5'-cyclic-GMP phosphodiesterase]] | [[Category: 3',5'-cyclic-GMP phosphodiesterase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Hengming, K]] | [[Category: Hengming, K]] | ||
[[Category: Howard, R]] | [[Category: Howard, R]] | ||
Revision as of 11:21, 5 January 2022
Crystal Structure of PDE5A1 catalytic domain in complex with Vardenafil
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Categories: 3',5'-cyclic-GMP phosphodiesterase | Homo sapiens | Large Structures | Hengming, K | Howard, R | Huanchen, W | Mengchun, Y | Sharron, H F | Allosteric enzyme | Alternative splicing | Cgmp phosphodiesterase | Cgmp-binding | Hydrolase | Levitratm | Magnesium | Metal-binding | Nucleotide-binding | Pde5-inhibitor potency | Phosphorylation | Polymorphism | Sildenafil | Vardenafil | Zinc

