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1lvz

METARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN

Method: SOLUTION NMR Dmax: 21.5 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Guanine nucleotide-binding protein G(T), alpha-1 subunit

Bos taurus

UniProt P04695

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 339–349 Fragment：S2 Peptide, Residues 339-349 Mutation：K340R, C346S No other associated polymer 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

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 1LVZ 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 experimental conditions 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method 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
1FQK CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)] Deposited 2000-09-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
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 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
1FQK CRYSTAL STRUCTURE OF THE HETERODIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)] Deposited 2000-09-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 26–215（190 aa） Fragment：UNP P04695 residues 26-215 and 295-350 linked via UNP P10824 residues 220-298
Chain C 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 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
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 method 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
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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 method 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 29 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 1–11； UniProt 339–349

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1lvz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lvz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lvz
Deposition date deposition_date2002-05-30
Structure title titleMETARHODOPSIN II BOUND STRUCTURE OF C-TERMINAL PEPTIDE OF ALPHA-SUBUNIT OF TRANSDUCIN
Keywords keywordsalpha helix, rhodopsin-transducin complex, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier5.29 Å
Radius of gyration Rg (electron density) rg_electron6.05 Å
Forward intensity I(0) i09643600.00
Molecular weight molecular_weight25829.0 kDa
Excluded volume excluded_volume32517 ų
Envelope volume envelope_volume2919 ų
Hydration-shell volume shell_volume3937 ų
Envelope diameter envelope_diameter23.2 Å
Shell Rg shell_rg11.56 Å
Envelope Rg envelope_rg7.48 Å
Shape Rg shape_rg5.99 Å
Total Rg total_rg6.57 Å
Total atoms total_atoms3700
Residues n_residues220
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax21.5 Å
Rg (real space) rg_real5.30 Å
Rg uncertainty (real space) rg_real_error0.43 Å
I(0) (real space) i0_real9.6440e+06
I(0) uncertainty (real space) i0_real_error1.0230e+05
Rg (reciprocal space) rg_reciprocal5.30 Å
I(0) (reciprocal space) i0_reciprocal9644000.0000
Solution quality estimate total_estimate0.7010
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary6.0 Å
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.919
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha364.4000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.601; Stabil: 0.989; Sysdev: 1.000; Positv: 1.000; Valcen: 0.337; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lvza_
Class classj — Peptides
Fold Fold foldj.56 — Transducin alpha-1 subunit rhodopsin binding domain (res. 340-350)
Superfamily Superfamily superfamilyj.56.1 — Transducin alpha-1 subunit rhodopsin binding domain (res. 340-350)
Family Family familyj.56.1.1 — Transducin alpha-1 subunit rhodopsin binding domain (res. 340-350)
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8. Citations (1)

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9. Files and Curves (10)