Opsin/G(alpha) peptide complex stabilized by nonyl-glucoside. Determined by X-ray diffraction at 2.29 Å resolution. Released 4 Nov 2015.
Explore 4X1H in 3D Show helices and sheets RCSB PDB PDBe
4X1H contains 19 α-helices and 4 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 | 4-6 | 3 | 1 |
| β-strand | 9-11 | 3 | 1 |
| α-helix | 34-64 | 31 | |
| α-helix | 66-68 | 3 | |
| α-helix | 71-73 | 3 | |
| α-helix | 74-86 | 13 | |
| α-helix | 87-91 | 5 | |
| α-helix | 92-98 | 7 | |
| α-helix | 106-140 | 35 | |
| 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 | 214-235 | 22 | |
| α-helix | 241-277 | 37 | |
| α-helix | 285-296 | 12 | |
| α-helix | 298-303 | 6 | |
| α-helix | 304-308 | 5 | |
| α-helix | 311-321 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 341-346 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rhodopsin | A | protein | 348 | Bos taurus | P02699 (AlphaFold model) |
| C-terminal derived peptide of guanine nucleotide-binding protein G(t) subunit alpha-1 | C | protein | 11 | Bos taurus |
>4X1H_1 Rhodopsin (chains A) MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLY VTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIP EGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAV YNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
>4X1H_2 C-terminal derived peptide of guanine nucleotide-binding protein G(t) subunit alpha-1 (chains C) VLEDLKSCGLF
The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation. Blankenship, E., Vahedi-Faridi, A., Lodowski, D.T. Structure (2015) 23:2358-2364. DOI 10.1016/j.str.2015.09.015 · 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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