5DO9: Regulator of G protein signaling 8
Structure of regulator of G protein signaling 8 (RGS8) in complex with AlF4-activated Galpha-q. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Jan 2016.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organisms
- Mus musculus, Homo sapiens
- Chains
- 6
- Atoms
- 11,425
- Mol. weight
- 159.56 kDa
- Ligands
- MG, ALF, GDP
- Released
- 20 Jan 2016
Explore 5DO9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5DO9 contains 99 α-helices and 24 β-strands across 6 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.
Chain A: 22 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 1 |
| α-helix | 52-63 | 12 | |
| α-helix | 69-73 | 5 | |
| α-helix | 76-96 | 21 | |
| α-helix | 99-101 | 3 | |
| α-helix | 105-114 | 10 | |
| α-helix | 118-120 | 3 | |
| α-helix | 128-136 | 9 | |
| α-helix | 139-146 | 8 | |
| α-helix | 148-150 | 3 | |
| α-helix | 157-161 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-181 | 6 | |
| β-strand | 189-195 | 7 | 1 |
| β-strand | 200-206 | 7 | 1 |
| α-helix | 210-213 | 4 | |
| α-helix | 214-219 | 6 | |
| β-strand | 225-231 | 7 | 1 |
| α-helix | 232-236 | 5 | |
| β-strand | 238 | 1 | 2 |
| β-strand | 246 | 1 | 2 |
| α-helix | 247-260 | 14 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-274 | 7 | 1 |
| α-helix | 276-282 | 7 | |
| α-helix | 288-290 | 3 | |
| α-helix | 302-314 | 13 | |
| β-strand | 324-328 | 5 | 1 |
| α-helix | 334-343 | 10 | |
| α-helix | 344-348 | 5 | |
Chain B: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-52 | 8 | |
| α-helix | 57-62 | 6 | |
| α-helix | 64-77 | 14 | |
| α-helix | 81-92 | 12 | |
| α-helix | 98-108 | 11 | |
| α-helix | 109-113 | 5 | |
| α-helix | 125-135 | 11 | |
| α-helix | 144-153 | 10 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-162 | 4 | |
| α-helix | 166-169 | 4 | |
Chain C: 22 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 3 |
| α-helix | 52-63 | 12 | |
| α-helix | 69-73 | 5 | |
| α-helix | 76-96 | 21 | |
| α-helix | 106-114 | 9 | |
| α-helix | 118-120 | 3 | |
| α-helix | 128-137 | 10 | |
| α-helix | 139-145 | 7 | |
| α-helix | 148-150 | 3 | |
| α-helix | 157-161 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-181 | 6 | |
| β-strand | 189-195 | 7 | 3 |
| β-strand | 200-206 | 7 | 3 |
| α-helix | 210-213 | 4 | |
| α-helix | 216-219 | 4 | |
| β-strand | 225-231 | 7 | 3 |
| α-helix | 232-236 | 5 | |
| β-strand | 238 | 1 | 4 |
| β-strand | 246 | 1 | 4 |
| α-helix | 247-260 | 14 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-274 | 7 | 3 |
| α-helix | 276-282 | 7 | |
| α-helix | 288-290 | 3 | |
| α-helix | 302-314 | 13 | |
| α-helix | 322-323 | 2 | |
| β-strand | 324-328 | 5 | 3 |
| α-helix | 334-343 | 10 | |
| α-helix | 344-348 | 5 | |
Chain D: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-53 | 9 | |
| α-helix | 57-62 | 6 | |
| α-helix | 64-76 | 13 | |
| α-helix | 81-92 | 12 | |
| 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 | 166-169 | 4 | |
Chain E: 22 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 39-45 | 7 | 5 |
| α-helix | 52-63 | 12 | |
| α-helix | 69-73 | 5 | |
| α-helix | 76-96 | 21 | |
| α-helix | 99-101 | 3 | |
| α-helix | 105-114 | 10 | |
| α-helix | 118-120 | 3 | |
| α-helix | 128-137 | 10 | |
| α-helix | 139-146 | 8 | |
| α-helix | 148-150 | 3 | |
| α-helix | 157-161 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 176-181 | 6 | |
| β-strand | 189-196 | 8 | 5 |
| β-strand | 199-206 | 8 | 5 |
| α-helix | 210-213 | 4 | |
| α-helix | 214-219 | 6 | |
| β-strand | 225-231 | 7 | 5 |
| α-helix | 232-236 | 5 | |
| β-strand | 238 | 1 | 6 |
| β-strand | 246 | 1 | 6 |
| α-helix | 247-260 | 14 | |
| α-helix | 262-264 | 3 | |
| β-strand | 268-274 | 7 | 5 |
| α-helix | 276-282 | 7 | |
| α-helix | 288-290 | 3 | |
| α-helix | 302-314 | 13 | |
| β-strand | 324-328 | 5 | 5 |
| α-helix | 334-343 | 10 | |
| α-helix | 344-348 | 5 | |
Chain F: 11 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 45-53 | 9 | |
| α-helix | 57-61 | 5 | |
| α-helix | 64-77 | 14 | |
| α-helix | 81-92 | 12 | |
| α-helix | 98-108 | 11 | |
| α-helix | 109-113 | 5 | |
| α-helix | 125-136 | 12 | |
| α-helix | 144-153 | 10 | |
| α-helix | 154-158 | 5 | |
| α-helix | 159-163 | 5 | |
| α-helix | 166-172 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Guanine nucleotide-binding protein G(q) subunit alpha | A, C, E | protein | 314 | Mus musculus | P21279 (AlphaFold model) |
| Regulator of G-protein signaling 8 | B, D, F | protein | 134 | Homo sapiens | P57771 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>5DO9_1 Guanine nucleotide-binding protein G(q) subunit alpha (chains A, C, E)
RRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDT
LKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDS
TKYYLNDLDRVADPSYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKW
IHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKK
DLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTEN
IRFVFAAVKDTILQ
Sequence of entity 2 (B, D, F), FASTA
>5DO9_2 Regulator of G-protein signaling 8 (chains B, D, F)
SMLKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTA
KLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSY
PRFLRSKMYLDLLS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 3 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 3 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 3 |
Primary citation
Structure of the Regulator of G Protein Signaling 8 (RGS8)-G alpha q Complex: MOLECULAR BASIS FOR G alpha SELECTIVITY. Taylor, V.G., Bommarito, P.A., Tesmer, J.J. J Biol Chem (2016) 291:5138-5145. DOI 10.1074/jbc.M115.712075 · PubMed
Other PDB entries of the same protein (UniProt P21279 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7SQ2 2.6 Å, Reprocessed and refined structure of Phospholipase C-beta and Gq signaling complex
- 4EKD 2.71 Å, Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine…
- 8YFS 2.8 Å, MRGPRE-Gq-scFv16-complex
- 3AH8 2.9 Å, Structure of heterotrimeric G protein Galpha-q beta gamma in complex with an inhibitor…
- 4QJ3 3.0 Å, Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with…
- 2BCJ 3.06 Å, Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and…
- 4QJ4 3.3 Å, Structure of a fragment of human phospholipase C-beta3 delta472-569, bound to IP3 and in…
- 4QJ5 3.41 Å, Structure of a fragment of human phospholipase C-beta3 delta472-581, bound to IP3 and in…
- 2RGN 3.5 Å, Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA
- 4GNK 4.0 Å, Crystal structure of Galphaq in complex with full-length human PLCbeta3
- 4EKC 7.4 Å, Structure of human regulator of G protein signaling 2 (RGS2) in complex with murine…
Browse structure collections
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