Crystal structure of the constitutively active E113Q,D2C,D282C rhodopsin mutant with bound galphact peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 16 Mar 2011.
Explore 2X72 in 3D Show helices and sheets RCSB PDB PDBe
2X72 contains 18 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 | 15-17 | 3 | |
| α-helix | 34-64 | 31 | |
| α-helix | 66-68 | 3 | |
| α-helix | 71-73 | 3 | |
| α-helix | 74-85 | 12 | |
| α-helix | 86-92 | 7 | |
| α-helix | 93-98 | 6 | |
| α-helix | 106-140 | 35 | |
| α-helix | 150-168 | 19 | |
| α-helix | 170-173 | 4 | |
| β-strand | 178-181 | 4 | 2 |
| β-strand | 186-189 | 4 | 2 |
| α-helix | 200-208 | 9 | |
| α-helix | 209-213 | 5 | |
| α-helix | 214-235 | 22 | |
| α-helix | 241-276 | 36 | |
| α-helix | 285-296 | 12 | |
| α-helix | 298-306 | 9 | |
| α-helix | 311-321 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 341-347 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rhodopsin | A | protein | 349 | BOS TAURUS | P02699 (AlphaFold model) |
| Guanine nucleotide-binding protein g(t) subunit alpha-1 | B | protein | 11 | BOS TAURUS | P04695 (AlphaFold model) |
>2X72_1 RHODOPSIN (chains A) XMCGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTL YVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLQGFFATL GGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYI PEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQE SATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSCFGPIFMTIPAFFAKTSA VYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
>2X72_2 GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-1 (chains B) ILENLKDCGLF
| ID | Name | Formula | Copies |
|---|---|---|---|
| PEF | Di-palmitoyl-3-sn-phosphatidylethanolamine | C37 H74 N O8 P | 1 |
| LPP | 2-(hexadecanoyloxy)-1-[(phosphonooxy)methyl]ethyl hexadecanoate | C35 H69 O8 P | 1 |
| RET | Retinal | C20 H28 O | 1 |
| PLM | Palmitic acid | C16 H32 O2 | 2 |
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 1 |
Water and common crystallization additives (ACT) are not listed.
The Structural Basis of Agonist Induced Activation in Constitutively Active Rhodopsin. Standfuss, J., Edwards, P.C., Dantona, A. et al. Nature (2011) 471:656. DOI 10.1038/NATURE09795 · 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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