1got

HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

GT-ALPHA/GI-ALPHA CHIMERA

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–349 Non-standard monomer:Yes (specific site not provided by mmCIF) GT-BETA × 1 (P62871) GT-GAMMA × 1 (P02698) 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

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.

16 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBT1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–350; UniProt 1–349

GT-BETA

Bos taurus

UniProt P62871

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–340 Not recorded GT-ALPHA/GI-ALPHA CHIMERA × 1 (P04695) GT-GAMMA × 1 (P02698) 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

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.

72 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

GT-GAMMA

Bos taurus

UniProt P02698

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–65 Not recorded GT-ALPHA/GI-ALPHA CHIMERA × 1 (P04695) GT-BETA × 1 (P62871) 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

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.

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG1_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 9–73; UniProt 1–65

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 1got

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1got
Deposition date deposition_date1996-08-07
Structure title titleHETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS
Keywords keywordsCOMPLEX (GTP-BINDING-TRANSDUCER), G PROTEIN, HETEROTRIMER SIGNAL TRANSDUCTION, COMPLEX (GTP-BINDING-TRANSDUCER) complex; COMPLEX (GTP-BINDING/TRANSDUCER)
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.92
Radius of gyration Rg (electron density) rg_electron29.17
Forward intensity I(0) i0122442000.00
Molecular weight molecular_weight83883.0 kDa
Excluded volume excluded_volume103240 ų
Envelope volume envelope_volume128300 ų
Hydration-shell volume shell_volume36722 ų
Envelope diameter envelope_diameter101.8
Shell Rg shell_rg36.34
Envelope Rg envelope_rg28.89
Shape Rg shape_rg29.15
Total Rg total_rg29.84
Total atoms total_atoms5832
Residues n_residues723
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax94.2
Rg (real space) rg_real29.87
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.2240e+08
I(0) uncertainty (real space) i0_real_error1.8430e+06
Rg (reciprocal space) rg_reciprocal29.89
I(0) (reciprocal space) i0_reciprocal122400000.0000
Solution quality estimate total_estimate0.9035
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.4
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18260000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.944; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1gota1
Class classa — All alpha proteins
Fold Fold folda.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamilya.66.1 — Transducin (alpha subunit), insertion domain
Family Family familya.66.1.1 — Transducin (alpha subunit), insertion domain
Domain ID domain_idd1gota2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1gotb_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat
Domain ID domain_idd1gotg_
Class classa — All alpha proteins
Fold Fold folda.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamilya.137.3 — Transducin (heterotrimeric G protein), gamma chain
Family Family familya.137.3.1 — Transducin (heterotrimeric G protein), gamma chain

CATH v4.4 (4 domains)

Domain ID domain_id1gotA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1gotA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id1gotB00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id1gotG00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology260 — G Protein Gi Gamma 2
Homologous superfamily homologous superfamily10 — Transducin (heterotrimeric G protein), gamma chain

8. Citations (5)

9. Files and Curves (10)