The crystal structure of the human G-protein subunit alpha (GNAI3) in complex with an engineered regulator of G-protein signaling type 2 domain (RGS2). Determined by X-ray diffraction at 2.8 Å resolution. Released 4 Nov 2008.
Explore 2V4Z in 3D Show helices and sheets RCSB PDB PDBe
2V4Z contains 28 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 | 33-39 | 7 | 1 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-91 | 22 | |
| α-helix | 100-113 | 14 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-156 | 5 | |
| α-helix | 159-162 | 4 | |
| α-helix | 171-176 | 6 | |
| β-strand | 184-190 | 7 | 1 |
| β-strand | 195-201 | 7 | 1 |
| α-helix | 205-214 | 10 | |
| 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 | 271-277 | 7 | |
| 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 | 75-79 | 5 | |
| α-helix | 84-89 | 6 | |
| α-helix | 91-103 | 13 | |
| α-helix | 108-119 | 12 | |
| α-helix | 125-139 | 15 | |
| α-helix | 152-160 | 9 | |
| α-helix | 171-180 | 10 | |
| α-helix | 181-185 | 5 | |
| α-helix | 186-191 | 6 | |
| α-helix | 193-198 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein g(k) subunit alpha | A | protein | 350 | HOMO SAPIENS | P08754 (AlphaFold model) |
| Regulator of G-protein signaling 2 | B | protein | 142 | HOMO SAPIENS | P41220 (AlphaFold model) |
>2V4Z_1 GUANINE NUCLEOTIDE-BINDING PROTEIN G(K) SUBUNIT ALPHA (chains A) SMTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGY SEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTP ELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKT TGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN RMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAA YIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKES
>2V4Z_2 REGULATOR OF G-PROTEIN SIGNALING 2 (chains B) SNAKPSPEEAQLWSEAFDELLASKYGLAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQK LSSKARKIYTDFIEKEAPKEINIDFQTKTLIAQNIQEATSGCFTTAQKRVYSLMENDSYP RFLKSEFYQDLCKKPQITTEPH
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| ALF | Tetrafluoroaluminate ion | Al F4 | 1 |
| MG | Magnesium ion | Mg | 1 |
Structural Determinants of G-Protein Alpha Subunit Selectivity by Regulator of G-Protein Signaling 2(Rgs2). Kimple, A.J., Soundararajan, M., Hutsell, S.Q. et al. J Biol Chem (2009) 284:19402. DOI 10.1074/JBC.M109.024711 · 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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