A Galpha P-loop mutation prevents transition to the activated state: G42R bound to RGS14 GoLoco. Determined by X-ray diffraction at 2.8 Å resolution. Released 1 Feb 2012.
Explore 3QI2 in 3D Show helices and sheets RCSB PDB PDBe
3QI2 contains 45 α-helices and 12 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 | 32-39 | 8 | 1 |
| α-helix | 46-56 | 11 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-90 | 21 | |
| α-helix | 93-95 | 3 | |
| α-helix | 100-113 | 14 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-141 | 8 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-157 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 171-176 | 6 | |
| β-strand | 184-191 | 8 | 1 |
| β-strand | 194-201 | 8 | 1 |
| α-helix | 208-215 | 8 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-230 | 4 | |
| α-helix | 232-235 | 4 | |
| α-helix | 242-255 | 14 | |
| 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 | 320-323 | 4 | 1 |
| α-helix | 329-345 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 36-40 | 5 | 2 |
| α-helix | 46-56 | 11 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-90 | 21 | |
| α-helix | 100-111 | 12 | |
| 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 | 171-176 | 6 | |
| β-strand | 186-190 | 5 | 2 |
| β-strand | 195-200 | 6 | 2 |
| α-helix | 205-207 | 3 | |
| α-helix | 212-215 | 4 | |
| β-strand | 220-226 | 7 | 2 |
| α-helix | 227-231 | 5 | |
| α-helix | 232-234 | 3 | |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| β-strand | 263-269 | 7 | 2 |
| α-helix | 271-277 | 7 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-308 | 13 | |
| β-strand | 319-323 | 5 | 2 |
| α-helix | 329-344 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 497-507 | 11 | |
| α-helix | 525-527 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 501-507 | 7 | |
| α-helix | 521-523 | 3 | |
| α-helix | 528-530 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide-binding protein G(i) subunit alpha-1 | A, B | protein | 328 | Homo sapiens | P63096 (AlphaFold model) |
| Regulator of G-protein signaling 14 | C, D | protein | 36 | O43566 (AlphaFold model) |
>3QI2_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A, B) SNAGAREVKLLLLGARESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIR AMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREY QLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRS ERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIIL FLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCA TDTKNVQFVFDAVTDVIIKNNLKDCGLF
>3QI2_2 Regulator of G-protein signaling 14 (chains C, D) DIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
Water and common crystallization additives (SO4, GOL) are not listed.
A P-loop Mutation in Galpha Subunits Prevents Transition to the Active State: Implications for G-protein Signaling in Fungal Pathogenesis. Bosch, D.E., Willard, F.S., Ramanujam, R. et al. PLoS Pathog (2012) 8:e1002553-e1002553. DOI 10.1371/journal.ppat.1002553 · PubMed
Other PDB entries of the same protein (UniProt P63096 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3QI2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.