Structure of PDE6C in complex with the rod inhibitory p gamma subunit with disordered GafA region. Determined by electron microscopy at 3.1 Å resolution. Released 18 Dec 2024.
Explore 9CXJ in 3D Show helices and sheets RCSB PDB PDBe
9CXJ contains 74 α-helices and 20 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 | 232-250 | 19 | |
| α-helix | 257-267 | 11 | |
| β-strand | 276-282 | 7 | 1 |
| α-helix | 283 | 1 | |
| α-helix | 290-298 | 9 | |
| β-strand | 308 | 1 | 2 |
| β-strand | 314 | 1 | 2 |
| β-strand | 317-324 | 8 | 1 |
| β-strand | 330-335 | 6 | 1 |
| α-helix | 348-355 | 8 | |
| β-strand | 358-362 | 5 | 1 |
| β-strand | 386-393 | 8 | 1 |
| β-strand | 399-405 | 7 | 1 |
| α-helix | 412-414 | 3 | |
| α-helix | 416-460 | 45 | |
| α-helix | 462-463 | 2 | |
| α-helix | 464-470 | 7 | |
| α-helix | 473-477 | 5 | |
| α-helix | 487-497 | 11 | |
| α-helix | 499-500 | 2 | |
| α-helix | 518-531 | 14 | |
| α-helix | 542-555 | 14 | |
| α-helix | 564-579 | 16 | |
| α-helix | 583-586 | 4 | |
| α-helix | 589-599 | 11 | |
| α-helix | 611-617 | 7 | |
| α-helix | 620-624 | 5 | |
| α-helix | 629-643 | 15 | |
| α-helix | 655-669 | 15 | |
| α-helix | 670-672 | 3 | |
| α-helix | 674-692 | 19 | |
| α-helix | 697-706 | 10 | |
| α-helix | 708-723 | 16 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-755 | 25 | |
| α-helix | 759-761 | 3 | |
| α-helix | 766-771 | 6 | |
| α-helix | 772-779 | 8 | |
| α-helix | 780-784 | 5 | |
| α-helix | 785-794 | 10 | |
| α-helix | 796-798 | 3 | |
| α-helix | 799-824 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 232-250 | 19 | |
| α-helix | 257-267 | 11 | |
| α-helix | 269-272 | 4 | |
| β-strand | 274 | 1 | 3 |
| β-strand | 276-282 | 7 | 4 |
| α-helix | 283 | 1 | |
| α-helix | 290-298 | 9 | |
| α-helix | 302-304 | 3 | |
| β-strand | 308 | 1 | 5 |
| β-strand | 314 | 1 | 5 |
| β-strand | 317-324 | 8 | 4 |
| β-strand | 330-335 | 6 | 4 |
| α-helix | 342-345 | 4 | |
| α-helix | 348-355 | 8 | |
| β-strand | 358-362 | 5 | 4 |
| α-helix | 364-366 | 3 | |
| β-strand | 386-393 | 8 | 4 |
| β-strand | 399-405 | 7 | 4 |
| β-strand | 408 | 1 | 3 |
| α-helix | 416-460 | 45 | |
| α-helix | 462-463 | 2 | |
| α-helix | 464-468 | 5 | |
| α-helix | 473-477 | 5 | |
| α-helix | 487-495 | 9 | |
| α-helix | 503-505 | 3 | |
| α-helix | 518-531 | 14 | |
| α-helix | 542-555 | 14 | |
| α-helix | 564-579 | 16 | |
| α-helix | 583-586 | 4 | |
| α-helix | 589-600 | 12 | |
| α-helix | 611-617 | 7 | |
| α-helix | 620-624 | 5 | |
| α-helix | 629-643 | 15 | |
| α-helix | 655-670 | 16 | |
| α-helix | 674-691 | 18 | |
| α-helix | 697-706 | 10 | |
| α-helix | 708-723 | 16 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-756 | 26 | |
| α-helix | 759-761 | 3 | |
| α-helix | 766-771 | 6 | |
| α-helix | 772-779 | 8 | |
| α-helix | 780-784 | 5 | |
| α-helix | 785-794 | 10 | |
| α-helix | 796-798 | 3 | |
| α-helix | 799-822 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-31 | 3 | 4 |
| α-helix | 32-34 | 3 | |
| α-helix | 75-83 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' | A, B | protein | 843 | Homo sapiens | P51160 (AlphaFold model) |
| Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma | C, D | protein | 99 | Bos taurus | P04972 (AlphaFold model) |
>9CXJ_1 Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' (chains A, B) GPTSGDYKDDDDKGGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSS MSFSELTQVEESALCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGI PEVASRLLDVTPTSKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDF MDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLH HTSYMYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKE KEFYDEWPIKLGEVEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISG LPTYVAENGFICNMMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYN RKDGKPFDEHDEYITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEI KSILKFQEKLNVDVIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIR LFFEINVVEKFKVPVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYY TDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESL NIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVD PTKKEIIMAMMMTACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRN KRDELPKLQVGFIDFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIE EEA
>9CXJ_2 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (chains C, D) MVGYPYDVPDYAMNLEPPKAEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQ GFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII
Structural and functional dynamics of human cone cGMP-phosphodiesterase important for photopic vision. Singh, S., Srivastava, D., Boyd, K. et al. Proc Natl Acad Sci U S A (2025) 122:e2419732121-e2419732121. DOI 10.1073/pnas.2419732121 · PubMed
Other PDB entries of the same protein (UniProt P51160 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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