;Guanine nucleotide-binding protein G(t) subunit alpha-1,Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(t) subunit alpha-1 ;
Bos taurus
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain A; UniProt 26–215 Chain A; UniProt 295–350 | Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298 | Regulator of G-protein signaling 9 × 1 (O46469) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;10.5% PEG8000, 110mM magnesium acetate, 50mM Tris pH 8.5, 0.2% beta-ME, VAPOR DIFFUSION, HANGING DROP, temperature 277K | Resolution 2.30 Å R-free 0.268 |
| 2 | Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count | Chain C; UniProt 26–215 Chain C; UniProt 295–350 | Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298 | Regulator of G-protein signaling 9 × 1 (O46469) MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;10.5% PEG8000, 110mM magnesium acetate, 50mM Tris pH 8.5, 0.2% beta-ME, VAPOR DIFFUSION, HANGING DROP, temperature 277K | Resolution 2.30 Å R-free 0.268 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 1FQK | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1AQG NMR STRUCTURE OF THE RHODOPSIN-BOUND C-TERMINAL PEPTIDE OF THE TRANSDUCIN ALPHA-SUBUNIT, 20 STRUCTURES Deposited 1997-07-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
339–349(11 aa)
Fragment:RHODOPSIN BINDING DOMAIN, RESIDUES 340-350
|
Not recorded | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 7.5;274 K;Ionic strength (raw mmCIF value) 120;Pressure AMBIENT
NMR sample composition
20 mM sodium phosphate, 100 mM KCl, 0.1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
|
Resolution not provided |
| 1FQJ CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)] Deposited 2000-09-05 | Different oligomeric state Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Heteromer;Protein × 3 PDB declaration: trimeric |
Chain A
26–215(190 aa)
Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298
Chain A
295–350(56 aa)
Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298
|
Not recorded | MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 9;277 K;15.0% PEG8000, 200mM Tris pH9.0, 0.2% beta-ME, 1mM (NH4)2WS4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.02 Å R-free 0.265 |
| 1FQJ CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)] Deposited 2000-09-05 | Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Heteromer;Protein × 2 PDB declaration: dimeric |
Chain D
26–215(190 aa)
Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298
Chain D
295–350(56 aa)
Fragment:UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298
|
Not recorded | MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 9;277 K;15.0% PEG8000, 200mM Tris pH9.0, 0.2% beta-ME, 1mM (NH4)2WS4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.02 Å R-free 0.265 |
| 1GOT HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS Deposited 1996-08-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric |
Chain A
1–349(349 aa)
|
Non-standard monomer:Yes (specific site not provided by mmCIF) | GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;10 MG/ML OF HETEROTRIMERIC COMPLEX WERE MIXED 1:1 WITH WELL SOLUTION CONTAINING 10% PEG-8000, 50 MM TRIS, PH 8.0, 10% GLYCEROL, 50 MM NACL, .1 MM MERCAPTOETHANOL. MIXTURE EQUILIBRATED VS WELL SOLUTION IN HANGING DROPS AT 4 DEGREES C., vapor diffusion - hanging drop, temperature 277K
|
Resolution 2.00 Å R-free 0.295 |
| 1LVZ METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN Deposited 2002-05-30 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
339–349(11 aa)
Fragment:S2 Peptide, Residues 339-349
|
Mutation:K340R, C346S | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.6;283 K;Ionic strength (raw mmCIF value) 10 mM HEPES, 20 mM KCl;Pressure ambient
NMR sample composition
2.6mM S2 peptide U-15N, 0.063mM rhodopsin as part of intact disk membranes from bovine retina; buffer: 10 mM HEPES, 20mM KCl, 0.05mM DTPA | 90% H2O/10% D2O
NMR sample composition
2.6mM S2 peptide U-15N, 13C, 0.063mM rhodopsin as part of intact disk membranes from bovine retina; buffer: 10 mM HEPES, 20mM KCl, 0.05mM DTPA | 90% H2O/10% D2O
|
Resolution not provided |
| 1TAD GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4- Deposited 1995-01-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain C
26–349(324 aa)
|
Not recorded | CA CALCIUM ION × 1 CAC CACODYLATE ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å R-free 0.266 |
| 1TAD GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4- Deposited 1995-01-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
26–349(324 aa)
|
Not recorded | CA CALCIUM ION × 1 CAC CACODYLATE ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å R-free 0.266 |
| 1TAD GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4- Deposited 1995-01-05 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain B
26–349(324 aa)
|
Not recorded | CA CALCIUM ION × 1 CAC CACODYLATE ION × 2 ALF TETRAFLUOROALUMINATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.70 Å R-free 0.266 |
| 1TAG STRUCTURAL DETERMINANTS FOR ACTIVATION OF THE ALPHA-SUBUNIT OF A HETEROTRIMERIC G PROTEIN Deposited 1994-11-23 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
26–349(324 aa)
|
Not recorded | MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.80 Å R-free 0.211 |
| 1TND THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S Deposited 1994-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
26–349(324 aa)
|
Not recorded | MG MAGNESIUM ION × 1 CAC CACODYLATE ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 1TND THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S Deposited 1994-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain B
26–349(324 aa)
|
Not recorded | MG MAGNESIUM ION × 1 CAC CACODYLATE ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 1TND THE 2.2 ANGSTROMS CRYSTAL STRUCTURE OF TRANSDUCIN-ALPHA COMPLEXED WITH GTP GAMMA S Deposited 1994-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric |
Chain C
26–349(324 aa)
|
Not recorded | MG MAGNESIUM ION × 1 CAC CACODYLATE ION × 2 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.20 Å |
| 2X72 CRYSTAL STRUCTURE OF THE CONSTITUTIVELY ACTIVE E113Q,D2C,D282C RHODOPSIN MUTANT WITH BOUND GALPHACT PEPTIDE. Deposited 2010-02-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain B
340–350(11 aa)
Fragment:RESIDUES 340-350
|
Mutation:YES | PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 2 BOG octyl beta-D-glucopyranoside × 2 PLM PALMITIC ACID × 4 RET RETINAL × 2 LPP 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE × 2 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.5;3.0-3.4 M AMMONIUM SULFATE, 100 MM SODIUM ACETATE PH 4.5
|
Resolution 3.00 Å R-free 0.244 |
| 3DQB Crystal structure of the active G-protein-coupled receptor opsin in complex with a C-terminal peptide derived from the Galpha subunit of transducin Deposited 2008-07-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 2 PDB declaration: dimeric |
Chain B
340–350(11 aa)
Fragment:C-terminal domain, UNP residues 340-350
|
Mutation:K341L | BOG octyl beta-D-glucopyranoside × 3 PLM PALMITIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6;277 K;AMMONIUM SULFATE, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 3.20 Å R-free 0.248 |
| 3PQR Crystal structure of Metarhodopsin II in complex with a C-terminal peptide derived from the Galpha subunit of transducin Deposited 2010-11-26 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 2 PDB declaration: dimeric |
Chain B
340–350(11 aa)
Fragment:C-terminal peptide (UNP residues 340-350)
|
Mutation:K341L,C347V | RET RETINAL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 BOG octyl beta-D-glucopyranoside × 2 PLM PALMITIC ACID × 1 SO4 SULFATE ION × 1 ACT ACETATE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.85 Å R-free 0.250 |
| 3PQR Crystal structure of Metarhodopsin II in complex with a C-terminal peptide derived from the Galpha subunit of transducin Deposited 2010-11-26 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Other combination Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain B
340–350(11 aa)
Fragment:C-terminal peptide (UNP residues 340-350)
|
Mutation:K341L,C347V | RET RETINAL × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 BOG octyl beta-D-glucopyranoside × 4 PLM PALMITIC ACID × 2 SO4 SULFATE ION × 2 ACT ACETATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.85 Å R-free 0.250 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric |
Chain C
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric |
Chain B
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric |
Chain A
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain A
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Insufficient information Homooligomer;Protein × 6 PDB declaration: hexameric |
Chain A
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain A
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Insufficient information Homooligomer;Protein × 3 PDB declaration: trimeric |
Chain A
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain A
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Insufficient information Homooligomer;Protein × 2 PDB declaration: dimeric |
Chain A
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain A
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain C
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 3V00 Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Deposited 2011-12-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 7 Insufficient information Homooligomer;Protein × 2 PDB declaration: dimeric |
Chain B
1–215(215 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
Chain B
295–350(56 aa)
Fragment:UNP P04695 1-215 & 295-350, UNP P10824 220-298
|
Mutation:G56P, K244H and D247N Mutation:G56P, K244H and D247N | GDP GUANOSINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 6.3;295 K;1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.90 Å R-free 0.272 |
| 4BEY Night blindness causing G90D rhodopsin in complex with GaCT2 peptide Deposited 2013-03-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 2 PDB declaration: dimeric |
Chain B
340–350(11 aa)
Fragment:RESIDUES 340-350
|
Mutation:YES | SO4 SULFATE ION × 1 ACT ACETATE ION × 1 PLM PALMITIC ACID × 1 BOG octyl beta-D-glucopyranoside × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.90 Å R-free 0.259 |
| 4J4Q Crystal structure of active conformation of GPCR opsin stabilized by octylglucoside Deposited 2013-02-07 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer;Protein × 2 PDB declaration: dimeric |
Chain B
340–350(11 aa)
Fragment:C-terminal derived peptide, UNP RESIDUES 340-350
|
Mutation:K341L, C347V | BOG octyl beta-D-glucopyranoside × 4 PLM PALMITIC ACID × 1 SO4 SULFATE ION × 2 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP;pH 5.6;277 K;AMMONIUM SULFATE, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|
Resolution 2.65 Å R-free 0.230 |
| 6OY9 Structure of the Rhodopsin-Transducin Complex Deposited 2019-05-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric |
Chain A
1–201(201 aa)
|
Not recorded | RET RETINAL × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.90 Å |
| 6OYA Structure of the Rhodopsin-Transducin-Nanobody Complex Deposited 2019-05-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric |
Chain A
1–201(201 aa)
|
Not recorded | RET RETINAL × 1 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.5
cryo-EM vitrification conditions
Cryogen ETHANE;Blot for 1 second before plunging; avoid light as much as possible.
|
Resolution 3.30 Å |
| 7JSN Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6 Deposited 2020-08-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric |
Chain E
1–215(215 aa)
Chain E
295–350(56 aa)
Chain F
1–215(215 aa)
Chain F
295–350(56 aa)
|
Mutation:R174C,Q200L Mutation:R174C,Q200L Mutation:R174C,Q200L Mutation:R174C,Q200L | ZN ZINC ION × 2 MG MAGNESIUM ION × 2 VDN 2-{2-ETHOXY-5-[(4-ETHYLPIPERAZIN-1-YL)SULFONYL]PHENYL}-5-METHYL-7-PROPYLIMIDAZO[5,1-F][1,2,4]TRIAZIN-4(1H)-ONE × 2 35G GUANOSINE-3',5'-MONOPHOSPHATE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 8;20 mM Tris pH 8.0, 5 mM MgCl2 and 1 uM vardenafil
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 3.20 Å |
16 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | GNAT1_BOVIN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 1–190; UniProt 26–215 Author chain A; PDBConstruct 270–325; UniProt 295–350 Author chain C; PDBConstruct 1–190; UniProt 26–215 Author chain C; PDBConstruct 270–325; UniProt 295–350 |