Structure of PDE6C in complex with the rod inhibitory p gamma subunit in the absence of added cGMP. Determined by electron microscopy at 3.0 Å resolution. Released 18 Dec 2024.
Explore 9CXI in 3D Show helices and sheets RCSB PDB PDBe
9CXI contains 95 α-helices and 40 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 | 55-69 | 15 | |
| α-helix | 76-91 | 16 | |
| β-strand | 94-104 | 11 | 1 |
| β-strand | 107-117 | 11 | 1 |
| α-helix | 123-126 | 4 | |
| β-strand | 127 | 1 | 1 |
| β-strand | 135-137 | 3 | 1 |
| α-helix | 141-149 | 9 | |
| β-strand | 153 | 1 | 1 |
| β-strand | 156 | 1 | 2 |
| α-helix | 158-160 | 3 | |
| α-helix | 167-172 | 6 | |
| β-strand | 178 | 1 | 2 |
| β-strand | 179-186 | 8 | 1 |
| β-strand | 189-197 | 9 | 1 |
| α-helix | 207-250 | 44 | |
| α-helix | 257-267 | 11 | |
| α-helix | 268-270 | 3 | |
| β-strand | 274 | 1 | 3 |
| β-strand | 276-282 | 7 | 4 |
| α-helix | 290-297 | 8 | |
| 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 | 1 | 6 |
| β-strand | 359-362 | 4 | 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 | 412-414 | 3 | |
| α-helix | 416-431 | 16 | |
| α-helix | 433-460 | 28 | |
| 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 | 534-537 | 4 | |
| 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 | 674-692 | 19 | |
| α-helix | 697-706 | 10 | |
| α-helix | 708-723 | 16 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-751 | 21 | |
| α-helix | 752-756 | 5 | |
| α-helix | 759-761 | 3 | |
| α-helix | 762-764 | 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 |
|---|---|---|---|
| α-helix | 52-67 | 16 | |
| α-helix | 68-70 | 3 | |
| α-helix | 76-91 | 16 | |
| β-strand | 94-104 | 11 | 7 |
| β-strand | 107-117 | 11 | 7 |
| α-helix | 123-126 | 4 | |
| β-strand | 127 | 1 | 7 |
| β-strand | 135-137 | 3 | 7 |
| α-helix | 141-149 | 9 | |
| β-strand | 153-155 | 3 | 7 |
| α-helix | 158-160 | 3 | |
| α-helix | 167-172 | 6 | |
| β-strand | 179-186 | 8 | 7 |
| β-strand | 189-197 | 9 | 7 |
| α-helix | 207-250 | 44 | |
| α-helix | 257-272 | 16 | |
| β-strand | 274 | 1 | 8 |
| β-strand | 276-282 | 7 | 9 |
| α-helix | 283 | 1 | |
| α-helix | 290-298 | 9 | |
| α-helix | 302-304 | 3 | |
| β-strand | 308 | 1 | 10 |
| β-strand | 314 | 1 | 10 |
| β-strand | 317-324 | 8 | 9 |
| β-strand | 331-335 | 5 | 9 |
| α-helix | 342-345 | 4 | |
| α-helix | 348-355 | 8 | |
| β-strand | 358 | 1 | 11 |
| β-strand | 359-362 | 4 | 9 |
| α-helix | 364-366 | 3 | |
| β-strand | 386-393 | 8 | 9 |
| β-strand | 399-405 | 7 | 9 |
| β-strand | 408 | 1 | 8 |
| α-helix | 416-460 | 45 | |
| α-helix | 462-463 | 2 | |
| α-helix | 464-468 | 5 | |
| α-helix | 473-477 | 5 | |
| α-helix | 487-494 | 8 | |
| α-helix | 499-500 | 2 | |
| 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 | 611-616 | 6 | |
| α-helix | 620-624 | 5 | |
| α-helix | 629-643 | 15 | |
| α-helix | 655-670 | 16 | |
| α-helix | 674-693 | 20 | |
| α-helix | 697-705 | 9 | |
| 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 |
|---|---|---|---|
| α-helix | 27-29 | 3 | |
| β-strand | 31 | 1 | 11 |
| α-helix | 35-38 | 4 | |
| α-helix | 77-83 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-29 | 3 | |
| β-strand | 31 | 1 | 6 |
| α-helix | 32-33 | 2 | |
| α-helix | 77-84 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' | A, B | protein | 843 | Homo sapiens | P51160 (AlphaFold model) |
| rod pg | C, D | protein | 99 | Mus musculus | P04972 (AlphaFold model) |
>9CXI_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
>9CXI_2 rod pg (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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