Structure of the Regulator of G-Protein Signaling Domain of RGS2. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Aug 2005.
Explore 2AF0 in 3D Show helices and sheets RCSB PDB PDBe
2AF0 contains 14 α-helices and 0 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 62-69 | 8 | |
| α-helix | 72-73 | 2 | |
| α-helix | 74-79 | 6 | |
| α-helix | 84-89 | 6 | |
| α-helix | 91-103 | 13 | |
| α-helix | 108-120 | 13 | |
| α-helix | 125-135 | 11 | |
| α-helix | 136-140 | 5 | |
| α-helix | 152-161 | 10 | |
| α-helix | 162-164 | 3 | |
| α-helix | 171-180 | 10 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 193-199 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulator of G-protein signaling 2 | A | protein | 146 | Homo sapiens | P41220 (AlphaFold model) |
>2AF0_1 Regulator of G-protein signaling 2 (chains A) ADLGTENLYFQSMKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACE DFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRV YSLMENNSYPRFLESEFYQDLCKKPQ
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 P41220 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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