Structure of PDE6C in complex with inhibitory cone p gamma in the presence of cGMP. Determined by electron microscopy at 3.0 Å resolution. Released 18 Dec 2024.
Explore 9CXG in 3D Show helices and sheets RCSB PDB PDBe
9CXG contains 98 α-helices and 38 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 | 56-69 | 14 | |
| α-helix | 76-91 | 16 | |
| β-strand | 93-104 | 12 | 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 | 142-149 | 8 | |
| β-strand | 153-155 | 3 | 1 |
| α-helix | 158-160 | 3 | |
| α-helix | 167-172 | 6 | |
| β-strand | 179-186 | 8 | 1 |
| β-strand | 189-199 | 11 | 1 |
| α-helix | 207-250 | 44 | |
| α-helix | 257-268 | 12 | |
| α-helix | 269-271 | 3 | |
| β-strand | 274 | 1 | 2 |
| β-strand | 276-282 | 7 | 3 |
| α-helix | 283 | 1 | |
| α-helix | 290-298 | 9 | |
| α-helix | 302-304 | 3 | |
| β-strand | 308 | 1 | 4 |
| β-strand | 314 | 1 | 4 |
| β-strand | 317-324 | 8 | 3 |
| β-strand | 330-335 | 6 | 3 |
| α-helix | 348-355 | 8 | |
| β-strand | 357-358 | 2 | 5 |
| β-strand | 359-362 | 4 | 3 |
| α-helix | 364-366 | 3 | |
| β-strand | 386-393 | 8 | 3 |
| β-strand | 399-406 | 8 | 3 |
| β-strand | 408 | 1 | 2 |
| α-helix | 413-414 | 2 | |
| α-helix | 416-431 | 16 | |
| α-helix | 433-460 | 28 | |
| α-helix | 462-463 | 2 | |
| α-helix | 464-470 | 7 | |
| α-helix | 474-477 | 4 | |
| α-helix | 487-497 | 11 | |
| α-helix | 499-500 | 2 | |
| α-helix | 518-531 | 14 | |
| α-helix | 535-538 | 4 | |
| α-helix | 542-555 | 14 | |
| α-helix | 564-579 | 16 | |
| α-helix | 583-586 | 4 | |
| α-helix | 589-601 | 13 | |
| α-helix | 611-616 | 6 | |
| α-helix | 620-624 | 5 | |
| α-helix | 629-643 | 15 | |
| α-helix | 655-670 | 16 | |
| α-helix | 674-692 | 19 | |
| α-helix | 697-705 | 9 | |
| α-helix | 708-723 | 16 | |
| α-helix | 725-728 | 4 | |
| α-helix | 731-754 | 24 | |
| 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 | 54-70 | 17 | |
| α-helix | 76-91 | 16 | |
| β-strand | 94-104 | 11 | 6 |
| β-strand | 107-117 | 11 | 6 |
| α-helix | 123-126 | 4 | |
| β-strand | 127 | 1 | 6 |
| α-helix | 128-129 | 2 | |
| β-strand | 135-137 | 3 | 6 |
| α-helix | 142-149 | 8 | |
| β-strand | 153-155 | 3 | 6 |
| α-helix | 158-160 | 3 | |
| α-helix | 167-172 | 6 | |
| β-strand | 179-186 | 8 | 6 |
| β-strand | 189-197 | 9 | 6 |
| α-helix | 207-250 | 44 | |
| α-helix | 257-272 | 16 | |
| β-strand | 274 | 1 | 7 |
| β-strand | 276-282 | 7 | 8 |
| α-helix | 283 | 1 | |
| α-helix | 290-298 | 9 | |
| α-helix | 302-304 | 3 | |
| β-strand | 308 | 1 | 9 |
| β-strand | 314 | 1 | 9 |
| β-strand | 317-324 | 8 | 8 |
| β-strand | 331-335 | 5 | 8 |
| α-helix | 348-355 | 8 | |
| β-strand | 358 | 1 | 10 |
| β-strand | 359-362 | 4 | 8 |
| α-helix | 364-366 | 3 | |
| β-strand | 386-393 | 8 | 8 |
| β-strand | 399-406 | 8 | 8 |
| β-strand | 408 | 1 | 7 |
| α-helix | 413-415 | 3 | |
| α-helix | 416-460 | 45 | |
| α-helix | 462-463 | 2 | |
| α-helix | 464-470 | 7 | |
| α-helix | 474-477 | 4 | |
| α-helix | 487-497 | 11 | |
| α-helix | 499-500 | 2 | |
| α-helix | 503-505 | 3 | |
| α-helix | 518-531 | 14 | |
| α-helix | 535-538 | 4 | |
| α-helix | 542-555 | 14 | |
| α-helix | 564-579 | 16 | |
| α-helix | 583-586 | 4 | |
| α-helix | 589-601 | 13 | |
| 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 | 731-755 | 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 | 799-822 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-29 | 4 | |
| β-strand | 31 | 1 | 10 |
| α-helix | 32-33 | 2 | |
| α-helix | 35-37 | 3 | |
| α-helix | 57-59 | 3 | |
| α-helix | 76-78 | 3 | |
| α-helix | 80-83 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 27-29 | 3 | |
| β-strand | 31-32 | 2 | 5 |
| α-helix | 33-34 | 2 | |
| α-helix | 36-39 | 4 | |
| α-helix | 77-83 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' | A, B | protein | 843 | Homo sapiens | P51160 (AlphaFold model) |
| cone P gamma | C, D | protein | 123 | Homo sapiens | P61249 (AlphaFold model) |
>9CXG_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
>9CXG_2 cone P gamma (chains C, D) MVAWSHPQFEKGGGSGGGSGGSAWSHPQFEKENLYFQGAMGSDSPSLSPPAPSQGPTTPR KGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQF GII
| ID | Name | Formula | Copies |
|---|---|---|---|
| PCG | Cyclic guanosine monophosphate | C10 H12 N5 O7 P | 2 |
| ZN | Zinc ion | Zn | 2 |
| MG | Magnesium ion | Mg | 2 |
| 5GP | Guanosine-5'-monophosphate | C10 H14 N5 O8 P | 2 |
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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