9ax5

Cryo-EM structure of Phospholipase C epsilon PH-C terminus in complex with RhoA-GTP

Method: ELECTRON MICROSCOPY Dmax: 121.6 Å Quality: REASONABLE

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

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1

Rattus norvegicus

UniProt Q99P84

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 837–2281 Fragment:PH-C terminal residues 837-2281 Transforming protein RhoA × 1 (P61586) CA CALCIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLCE1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–1468; UniProt 837–2281

Transforming protein RhoA

Homo sapiens

UniProt P61586

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–193 Not recorded 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 × 1 (Q99P84) CA CALCIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

129 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 25–216; UniProt 2–193

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 9ax5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ax5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ax5
Deposition date deposition_date2024-03-05
Structure title titleCryo-EM structure of Phospholipase C epsilon PH-C terminus in complex with RhoA-GTP
Keywords keywordsGPCR signaling, complex, phospholipase, PIP2 hydrolysis, G protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.48
Radius of gyration Rg (electron density) rg_electron34.97
Forward intensity I(0) i0226477000.00
Molecular weight molecular_weight121560.0 kDa
Excluded volume excluded_volume152310 ų
Envelope volume envelope_volume197490 ų
Hydration-shell volume shell_volume47598 ų
Envelope diameter envelope_diameter129.1
Shell Rg shell_rg40.93
Envelope Rg envelope_rg35.10
Shape Rg shape_rg34.92
Total Rg total_rg35.54
Total atoms total_atoms8543
Residues n_residues1065
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 dmax121.6
Rg (real space) rg_real35.55
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real2.2650e+08
I(0) uncertainty (real space) i0_real_error4.0810e+06
Rg (reciprocal space) rg_reciprocal35.51
I(0) (reciprocal space) i0_reciprocal226500000.0000
Solution quality estimate total_estimate0.6858
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.8
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52130000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.973; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)