Crystal structure of bovine rhodopsin with beta-ionone. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Jan 2011.
Explore 3OAX in 3D Show helices and sheets RCSB PDB PDBe
3OAX contains 33 α-helices and 8 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 4-5 | 2 | 1 |
| β-strand | 10-11 | 2 | 1 |
| α-helix | 34-64 | 31 | |
| α-helix | 71-85 | 15 | |
| α-helix | 86-91 | 6 | |
| α-helix | 92-100 | 9 | |
| α-helix | 106-139 | 34 | |
| α-helix | 150-168 | 19 | |
| α-helix | 170-172 | 3 | |
| β-strand | 178-181 | 4 | 2 |
| β-strand | 186-189 | 4 | 2 |
| α-helix | 196-198 | 3 | |
| α-helix | 200-208 | 9 | |
| α-helix | 209-213 | 5 | |
| α-helix | 214-225 | 12 | |
| α-helix | 242-276 | 35 | |
| α-helix | 286-295 | 10 | |
| α-helix | 296-299 | 4 | |
| α-helix | 301-309 | 9 | |
| α-helix | 311-321 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 3 |
| β-strand | 10-11 | 2 | 3 |
| α-helix | 29-31 | 3 | |
| α-helix | 34-64 | 31 | |
| α-helix | 71-85 | 15 | |
| α-helix | 86-91 | 6 | |
| α-helix | 92-100 | 9 | |
| α-helix | 106-136 | 31 | |
| α-helix | 150-168 | 19 | |
| α-helix | 170-173 | 4 | |
| β-strand | 178-181 | 4 | 4 |
| β-strand | 186-189 | 4 | 4 |
| α-helix | 196-198 | 3 | |
| α-helix | 200-208 | 9 | |
| α-helix | 209-213 | 5 | |
| α-helix | 214-221 | 8 | |
| α-helix | 242-276 | 35 | |
| α-helix | 285-294 | 10 | |
| α-helix | 295-299 | 5 | |
| α-helix | 301-309 | 9 | |
| α-helix | 311-321 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rhodopsin | A, B | protein | 349 | Bos taurus | P02699 (AlphaFold model) |
>3OAX_1 Rhodopsin (chains A, B) XMNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTL YVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATL GGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYI PEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQE SATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSA VYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
| ID | Name | Formula | Copies |
|---|---|---|---|
| RET | Retinal | C20 H28 O | 2 |
| PLM | Palmitic acid | C16 H32 O2 | 4 |
| HG | Mercury (II) ion | Hg | 6 |
| ZN | Zinc ion | Zn | 7 |
| 4E6 | (4E,6E)-hexadeca-1,4,6-triene | C16 H28 | 2 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 1 |
| ID3 | (3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one | C13 H20 O | 2 |
| HTG | heptyl 1-thio-beta-D-glucopyranoside | C13 H26 O5 S | 4 |
Binding of more than one retinoid to visual opsins. Makino, C.L., Riley, C.K., Looney, J. et al. Biophys J (2010) 99:2366-2373. DOI 10.1016/j.bpj.2010.08.003 · PubMed
Other PDB entries of the same protein (UniProt P02699 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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