Crystal structure of chimeric PDE5/PDE6 catalytic domain complexed with sildenafil. Determined by X-ray diffraction at 2.87 Å resolution. Released 13 Oct 2009.
Explore 3JWQ in 3D Show helices and sheets RCSB PDB PDBe
3JWQ contains 90 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 537-545 | 9 | |
| α-helix | 568-581 | 14 | |
| α-helix | 584-588 | 5 | |
| α-helix | 592-604 | 13 | |
| α-helix | 615-629 | 15 | |
| α-helix | 635-637 | 3 | |
| α-helix | 640-652 | 13 | |
| α-helix | 662-667 | 6 | |
| α-helix | 672-675 | 4 | |
| α-helix | 680-693 | 14 | |
| α-helix | 706-721 | 16 | |
| α-helix | 725-740 | 16 | |
| α-helix | 749-764 | 16 | |
| α-helix | 766-769 | 4 | |
| α-helix | 772-795 | 24 | |
| α-helix | 803-805 | 3 | |
| α-helix | 807-812 | 6 | |
| α-helix | 813-820 | 8 | |
| α-helix | 821-825 | 5 | |
| α-helix | 826-835 | 10 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-857 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 537-545 | 9 | |
| α-helix | 551-554 | 4 | |
| α-helix | 568-581 | 14 | |
| α-helix | 584-588 | 5 | |
| α-helix | 592-604 | 13 | |
| α-helix | 615-630 | 16 | |
| α-helix | 635-637 | 3 | |
| α-helix | 640-652 | 13 | |
| α-helix | 662-667 | 6 | |
| α-helix | 671-675 | 5 | |
| α-helix | 680-693 | 14 | |
| α-helix | 706-721 | 16 | |
| α-helix | 725-740 | 16 | |
| α-helix | 749-764 | 16 | |
| α-helix | 766-769 | 4 | |
| α-helix | 772-796 | 25 | |
| α-helix | 803-805 | 3 | |
| α-helix | 813-820 | 8 | |
| α-helix | 821-825 | 5 | |
| α-helix | 826-835 | 10 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-856 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 538-545 | 8 | |
| α-helix | 551-554 | 4 | |
| α-helix | 568-581 | 14 | |
| α-helix | 584-588 | 5 | |
| α-helix | 592-604 | 13 | |
| α-helix | 615-629 | 15 | |
| α-helix | 635-637 | 3 | |
| α-helix | 640-652 | 13 | |
| α-helix | 662-667 | 6 | |
| α-helix | 672-675 | 4 | |
| α-helix | 680-693 | 14 | |
| α-helix | 706-721 | 16 | |
| α-helix | 725-740 | 16 | |
| α-helix | 749-764 | 16 | |
| α-helix | 766-769 | 4 | |
| α-helix | 772-795 | 24 | |
| α-helix | 803-805 | 3 | |
| α-helix | 810-812 | 3 | |
| α-helix | 813-820 | 8 | |
| α-helix | 821-825 | 5 | |
| α-helix | 826-835 | 10 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-856 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 538-545 | 8 | |
| α-helix | 568-581 | 14 | |
| α-helix | 584-588 | 5 | |
| α-helix | 592-604 | 13 | |
| α-helix | 615-629 | 15 | |
| α-helix | 635-637 | 3 | |
| α-helix | 640-652 | 13 | |
| α-helix | 662-667 | 6 | |
| α-helix | 671-674 | 4 | |
| α-helix | 680-693 | 14 | |
| α-helix | 706-721 | 16 | |
| α-helix | 725-740 | 16 | |
| α-helix | 749-764 | 16 | |
| α-helix | 766-769 | 4 | |
| α-helix | 772-795 | 24 | |
| α-helix | 799-801 | 3 | |
| α-helix | 803-805 | 3 | |
| α-helix | 807-812 | 6 | |
| α-helix | 813-820 | 8 | |
| α-helix | 821-825 | 5 | |
| α-helix | 826-835 | 10 | |
| α-helix | 837-839 | 3 | |
| α-helix | 840-857 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cGMP-specific 3',5'-cyclic phosphodiesterase catalytic domain, Cone cGMP-specific 3',5'-cyclic… | A, B, C, D | protein | 330 | Homo sapiens | O76074 (AlphaFold model), P51160 (AlphaFold model) |
>3JWQ_1 cGMP-specific 3',5'-cyclic phosphodiesterase catalytic domain, Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha chimera (chains A, B, C, D) GSHMEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQM KHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAA LSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYK TTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITK PWPIQQRIAELVATEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFIDFVCTQLYE ALTHVSEDCFPLLDGCRKNRQKWQALAEQQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
| MG | Magnesium ion | Mg | 4 |
| VIA | 5-{2-ethoxy-5-[(4-methylpiperazin-1-yl)sulfonyl]phenyl}-1-methyl-3-propyl-1H,6H… | C22 H30 N6 O4 S | 4 |
Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the gamma-subunit. Barren, B., Gakhar, L., Muradov, H. et al. EMBO J (2009) 28:3613-3622. DOI 10.1038/emboj.2009.284 · PubMed
Other PDB entries of the same protein (UniProt O76074 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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