Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3. Determined by X-ray diffraction at 2.71 Å resolution. Released 21 Nov 2006.
Explore 2IHB in 3D Show helices and sheets RCSB PDB PDBe
2IHB contains 30 α-helices and 8 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 | 34-39 | 6 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-67 | 5 | |
| α-helix | 70-91 | 22 | |
| α-helix | 93-95 | 3 | |
| α-helix | 100-109 | 10 | |
| α-helix | 111-114 | 4 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-156 | 5 | |
| α-helix | 159-163 | 5 | |
| α-helix | 171-175 | 5 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 205-208 | 4 | |
| α-helix | 211-214 | 4 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-231 | 5 | |
| β-strand | 233 | 1 | 2 |
| β-strand | 241 | 1 | 2 |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 1 |
| α-helix | 271-280 | 10 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 329-345 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-32 | 8 | |
| α-helix | 34-39 | 6 | |
| α-helix | 41-53 | 13 | |
| α-helix | 57-71 | 15 | |
| α-helix | 75-85 | 11 | |
| α-helix | 86-90 | 5 | |
| α-helix | 120-129 | 10 | |
| α-helix | 130-134 | 5 | |
| α-helix | 135-138 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(k) subunit alpha | A | protein | 323 | Homo sapiens | P08754 (AlphaFold model) |
| Regulator of G-protein signalling 10 | B | protein | 153 | Homo sapiens | O43665 (AlphaFold model) |
>2IHB_1 Guanine nucleotide-binding protein G(k) subunit alpha (chains A) KEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRL KIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDS ASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKW IHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKK DLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKN VQFVFDAVTDVIIKNNLKECGLY
>2IHB_2 Regulator of G-protein signalling 10 (chains B) SMSRKRPPSDIHDSDGSSSSSHQSLKSTAKWAASLENLLEDPEGVKRFREFLKKEFSEEN VLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKILEEPHPLMF QKLQDQIFNLMKYDSYSRFLKSDLFLKHKRTEE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ALF | Tetrafluoroaluminate ion | Al F4 | 1 |
| MG | Magnesium ion | Mg | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
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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