Crystal structure of the heterodimeric complex of human RGS8 and activated Gi alpha 3. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 Feb 2007.
Explore 2ODE in 3D Show helices and sheets RCSB PDB PDBe
2ODE contains 57 α-helices and 16 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 |
|---|---|---|---|
| β-strand | 34-39 | 6 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-91 | 22 | |
| α-helix | 100-110 | 11 | |
| α-helix | 121-131 | 11 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-162 | 4 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-231 | 5 | |
| β-strand | 233-234 | 2 | 2 |
| β-strand | 237-241 | 5 | 2 |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-278 | 8 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-346 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 47-52 | 6 | |
| α-helix | 57-61 | 5 | |
| α-helix | 64-76 | 13 | |
| α-helix | 80-92 | 13 | |
| α-helix | 98-108 | 11 | |
| α-helix | 109-113 | 5 | |
| α-helix | 125-134 | 10 | |
| α-helix | 144-153 | 10 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-164 | 6 | |
| α-helix | 166-174 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32-40 | 9 | 3 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-67 | 5 | |
| α-helix | 70-91 | 22 | |
| α-helix | 100-110 | 11 | |
| α-helix | 121-131 | 11 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-162 | 4 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 3 |
| β-strand | 194-201 | 8 | 3 |
| α-helix | 205-214 | 10 | |
| β-strand | 220-226 | 7 | 3 |
| α-helix | 227-231 | 5 | |
| β-strand | 233 | 1 | 4 |
| β-strand | 241 | 1 | 4 |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 3 |
| α-helix | 271-277 | 7 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 3 |
| α-helix | 329-345 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 57-62 | 6 | |
| α-helix | 64-76 | 13 | |
| α-helix | 80-92 | 13 | |
| α-helix | 98-108 | 11 | |
| α-helix | 109-113 | 5 | |
| α-helix | 125-134 | 10 | |
| α-helix | 144-153 | 10 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-163 | 5 | |
| α-helix | 166-170 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(k) subunit alpha | A, C | protein | 350 | Homo sapiens | P08754 (AlphaFold model) |
| Regulator of G-protein signaling 8 | B, D | protein | 141 | Homo sapiens | P57771 (AlphaFold model) |
>2ODE_1 Guanine nucleotide-binding protein G(k) subunit alpha (chains A, C) SMTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGY SEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTP ELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKT TGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN RMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAA YIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKES
>2ODE_2 Regulator of G-protein signaling 8 (chains B, D) SMLKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTA KLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSY PRFLRSKMYLDLLSQSQRRLS
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| MG | Magnesium ion | Mg | 2 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 2 |
Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Soundararajan, M., Willard, F.S., Kimple, A.J. et al. Proc Natl Acad Sci U S A (2008) 105:6457-6462. DOI 10.1073/pnas.0801508105 · PubMed
Other PDB entries of the same protein (UniProt P08754 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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