Structure of PDE5 PDE6 chimera. Determined by electron microscopy at 3.06 Å resolution. Released 6 May 2026.
Explore 10OZ in 3D Show helices and sheets RCSB PDB PDBe
10OZ contains 72 α-helices and 34 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 | 50-65 | 16 | |
| α-helix | 71-86 | 16 | |
| β-strand | 88-99 | 12 | 1 |
| β-strand | 102-109 | 8 | 1 |
| α-helix | 118-121 | 4 | |
| β-strand | 122 | 1 | 1 |
| α-helix | 125-127 | 3 | |
| β-strand | 130-132 | 3 | 1 |
| α-helix | 136-144 | 9 | |
| β-strand | 148-150 | 3 | 1 |
| α-helix | 162-167 | 6 | |
| β-strand | 174-181 | 8 | 1 |
| β-strand | 184-194 | 11 | 1 |
| α-helix | 202-245 | 44 | |
| α-helix | 252-262 | 11 | |
| β-strand | 269-277 | 9 | 2 |
| β-strand | 303 | 1 | 3 |
| β-strand | 309 | 1 | 3 |
| β-strand | 312-319 | 8 | 2 |
| β-strand | 325-330 | 6 | 2 |
| α-helix | 343-350 | 8 | |
| β-strand | 353 | 1 | 4 |
| β-strand | 354-357 | 4 | 2 |
| β-strand | 381-387 | 7 | 2 |
| β-strand | 396-403 | 8 | 2 |
| α-helix | 408-409 | 2 | |
| α-helix | 411-426 | 16 | |
| α-helix | 428-454 | 27 | |
| α-helix | 459-469 | 11 | |
| α-helix | 493-506 | 14 | |
| α-helix | 509-512 | 4 | |
| α-helix | 517-530 | 14 | |
| α-helix | 540-555 | 16 | |
| α-helix | 559-562 | 4 | |
| α-helix | 565-576 | 12 | |
| α-helix | 587-592 | 6 | |
| α-helix | 596-599 | 4 | |
| α-helix | 605-619 | 15 | |
| α-helix | 631-646 | 16 | |
| α-helix | 650-665 | 16 | |
| α-helix | 674-689 | 16 | |
| α-helix | 691-693 | 3 | |
| α-helix | 697-722 | 26 | |
| α-helix | 732-737 | 6 | |
| α-helix | 738-745 | 8 | |
| α-helix | 746-750 | 5 | |
| α-helix | 751-760 | 10 | |
| α-helix | 762-764 | 3 | |
| α-helix | 765-782 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 51-65 | 15 | |
| α-helix | 71-86 | 16 | |
| β-strand | 88-99 | 12 | 5 |
| β-strand | 102-109 | 8 | 5 |
| α-helix | 118-121 | 4 | |
| β-strand | 122 | 1 | 5 |
| α-helix | 125-127 | 3 | |
| β-strand | 130-132 | 3 | 5 |
| α-helix | 136-144 | 9 | |
| β-strand | 148-150 | 3 | 5 |
| α-helix | 162-167 | 6 | |
| β-strand | 174-181 | 8 | 5 |
| β-strand | 184-194 | 11 | 5 |
| α-helix | 202-245 | 44 | |
| α-helix | 252-261 | 10 | |
| α-helix | 264-267 | 4 | |
| β-strand | 269-277 | 9 | 6 |
| α-helix | 278 | 1 | |
| β-strand | 303 | 1 | 7 |
| β-strand | 309 | 1 | 7 |
| β-strand | 312-319 | 8 | 6 |
| β-strand | 325-330 | 6 | 6 |
| α-helix | 343-350 | 8 | |
| β-strand | 353 | 1 | 8 |
| β-strand | 354-357 | 4 | 6 |
| α-helix | 359-361 | 3 | |
| β-strand | 381-388 | 8 | 6 |
| β-strand | 394-403 | 10 | 6 |
| α-helix | 408-409 | 2 | |
| α-helix | 411-454 | 44 | |
| α-helix | 459-469 | 11 | |
| α-helix | 493-506 | 14 | |
| α-helix | 509-512 | 4 | |
| α-helix | 517-530 | 14 | |
| α-helix | 540-555 | 16 | |
| α-helix | 560-562 | 3 | |
| α-helix | 565-576 | 12 | |
| α-helix | 587-592 | 6 | |
| α-helix | 596-600 | 5 | |
| α-helix | 605-618 | 14 | |
| α-helix | 631-646 | 16 | |
| α-helix | 650-665 | 16 | |
| α-helix | 674-689 | 16 | |
| α-helix | 691-693 | 3 | |
| α-helix | 697-717 | 21 | |
| α-helix | 718-722 | 5 | |
| α-helix | 735-737 | 3 | |
| α-helix | 738-745 | 8 | |
| α-helix | 746-751 | 6 | |
| α-helix | 752-760 | 9 | |
| α-helix | 762-764 | 3 | |
| α-helix | 765-782 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-29 | 3 | |
| β-strand | 31 | 1 | 8 |
| α-helix | 32-33 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31 | 1 | 4 |
| α-helix | 34-37 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| cGMP-specific 3',5'-cyclic phosphodiesterase PDE5-PDE6 chimera | A, B | protein | 800 | Bos taurus | P16586 (AlphaFold model), Q28156 (AlphaFold model) |
| Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma | C, D | protein | 107 | Bos taurus | P04972 (AlphaFold model) |
>10OZ_1 cGMP-specific 3',5'-cyclic phosphodiesterase PDE5-PDE6 chimera (chains A, B) MGEISQETVEKYLEANPQFAKEYFNRKLQVEVPSGGAQAPASASFPGRTLAEEAALYLEL LEVLLEEAGSVELAAHRALQRLAQLLQADRCSMFLCRARNGTPEVASKLLDVTPTSKFED NLVVPDREAVFPLDVGIVGWVAHTKKTFNVPDVKKNSHFSDFMDKQTGYVTRNLLATPIV MGKEVLAVFMAVNKVDASEFSKQDEEVFSKYLSFVSIILKLHHTNYLYNIESRRSQILMW SANKVFEELTDVERQFHKALYTVRTYLNCERYSIGLLDMTKEKEFYDEWPVKLGEVEPYK GPKTPDGREVIFYKIIDYILHGKEEIKVIPTPPMDHWTLISGLPTYVAENGFICNMLNAP ADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEYDEHIAETL TQFLGWSLLNTDTYEKMNKLMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLK ITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCKWILSVKKNYRKNVAYHNW RHAFNTAQCMFAALKAGKIQKRLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQL YCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEF FELIMKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERK ELNIEPADLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQA LAEQQEKTLINGESSQTKRN
>10OZ_2 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (chains C, D) MGSSHHHHHHSSGLVPRGSHMNLEPPKAEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKS KPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
| MG | Magnesium ion | Mg | 2 |
| PCG | Cyclic guanosine monophosphate | C10 H12 N5 O7 P | 2 |
| VIA | 5-{2-ethoxy-5-[(4-methylpiperazin-1-yl)sulfonyl]phenyl}-1-methyl-3-propyl-1H,6H… | C22 H30 N6 O4 S | 2 |
Structural basis of phosphodiesterase-5 conformational organization revealed by a PDE6/PDE5 chimera. Srivastava, D., Singh, S., Yu, C. et al. J Biol Chem (2026) 302:111467-111467. DOI 10.1016/j.jbc.2026.111467 · PubMed
Other PDB entries of the same protein (UniProt P16586 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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