8uqo

PLCb3-Gbg-Gaq complex on membranes

Method: ELECTRON MICROSCOPY Dmax: 134.6 Å Quality: GOOD

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

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

Homo sapiens

UniProt P62873

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–340 Chain C; UniProt 1–340 Not recorded Guanine nucleotide-binding protein subunit gamma × 2 (G3V2N0) Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P50148) 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340 Author chain C; PDBConstruct 1–340; UniProt 1–340

Guanine nucleotide-binding protein subunit gamma

Homo sapiens

UniProt G3V2N0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 39–110 Chain G; UniProt 39–110 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P50148) 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name G3V2N0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 2–73; UniProt 39–110 Author chain G; PDBConstruct 2–73; UniProt 39–110

Guanine nucleotide-binding protein G(q) subunit alpha

Homo sapiens

UniProt P50148

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 7–359 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein subunit gamma × 2 (G3V2N0) 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAQ_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 3–355; UniProt 7–359

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Q; UniProt 10–1234 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 2 (P62873) Guanine nucleotide-binding protein subunit gamma × 2 (G3V2N0) Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P50148) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 4
Chains and sequence ranges Author chain Q; PDBConstruct 10–1234; UniProt 10–1234

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 8uqo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uqo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uqo
Deposition date deposition_date2023-10-24
最后修订 last_revision2023-12-06
Structure title titlePLCb3-Gbg-Gaq complex on membranes
Keywords keywordsPLCb3, Gbg, Gaq, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.07
Radius of gyration Rg (electron density) rg_electron42.48
Forward intensity I(0) i0589408000.00
Molecular weight molecular_weight198580.0 kDa
Excluded volume excluded_volume247810 ų
Envelope volume envelope_volume344530 ų
Hydration-shell volume shell_volume66807 ų
Envelope diameter envelope_diameter138.4
Shell Rg shell_rg48.50
Envelope Rg envelope_rg41.78
Shape Rg shape_rg42.48
Total Rg total_rg42.75
Total atoms total_atoms13958
Residues n_residues1823
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 dmax134.6
Rg (real space) rg_real42.90
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real5.8940e+08
I(0) uncertainty (real space) i0_real_error9.9870e+06
Rg (reciprocal space) rg_reciprocal43.07
I(0) (reciprocal space) i0_reciprocal589500000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.8
Skewness Skewness skewness0.079
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha156900000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)