9y7h

Gb1g2 crosslinked to PLCb3

Method: ELECTRON MICROSCOPY Dmax: 110.5 Å Quality: GOOD

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

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3

Homo sapiens

UniProt Q01970

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 10–882 Mutation:E60C, C193S, C221S, C358S, C516S, C824S, C834S Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) ME7 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione) × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 100 mM NaCl, 0.1 mM EDTA and 0.1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å

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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLCB3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–883; UniProt 10–882

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

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 8–339 Not recorded 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) ME7 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione) × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 100 mM NaCl, 0.1 mM EDTA and 0.1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å

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 1–332; UniProt 8–339

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Bos taurus

UniProt P63212

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 1–71 Not recorded 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) ME7 1,1'-ethane-1,2-diylbis(1H-pyrrole-2,5-dione) × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;20 mM HEPES pH 7.4, 100 mM NaCl, 0.1 mM EDTA and 0.1 mM EGTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 Å

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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

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 9y7h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y7h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y7h
Deposition date deposition_date2025-09-10
Structure title titleGb1g2 crosslinked to PLCb3
Keywords keywordsheterotrimeric G protein, phospholipase, lipase, calcium signaling, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.40
Radius of gyration Rg (electron density) rg_electron33.70
Forward intensity I(0) i0252871000.00
Molecular weight molecular_weight126850.0 kDa
Excluded volume excluded_volume158500 ų
Envelope volume envelope_volume209950 ų
Hydration-shell volume shell_volume51326 ų
Envelope diameter envelope_diameter113.9
Shell Rg shell_rg40.94
Envelope Rg envelope_rg33.34
Shape Rg shape_rg33.68
Total Rg total_rg34.30
Total atoms total_atoms17710
Residues n_residues1125
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 dmax110.5
Rg (real space) rg_real34.33
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real2.5290e+08
I(0) uncertainty (real space) i0_real_error4.0010e+06
Rg (reciprocal space) rg_reciprocal34.38
I(0) (reciprocal space) i0_reciprocal252900000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.9
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.440
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha74420000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)