9ci3

Structure of the LRRK2/14-3-3 complex

Method: ELECTRON MICROSCOPY Dmax: 146.4 Å Quality: GOOD

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

14-3-3 protein gamma

Homo sapiens

UniProt P61981

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 1–247 Chain C; UniProt 1–247 Not recorded Leucine-rich repeat serine/threonine-protein kinase 2 × 1 (Q5S007) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.96 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.

21 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433G_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 19–265; UniProt 1–247 Author chain C; PDBConstruct 19–265; UniProt 1–247

Leucine-rich repeat serine/threonine-protein kinase 2

Homo sapiens

UniProt Q5S007

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 1–2527 Mutation:R50H variant Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein gamma × 2 (P61981) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.96 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.

40 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LRRK2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 36–2562; UniProt 1–2527

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 9ci3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ci3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9ci3
Deposition date deposition_date2024-07-02
最后修订 last_revision2025-09-03
Structure title titleStructure of the LRRK2/14-3-3 complex
Keywords keywordsLRRK2, LRRK2 complex, LRRK2 14-3-3 complex, LRRK2 autoinhibited, TRANSFERASE, TRANSFERASE-SIGNALING PROTEIN complex; TRANSFERASE/SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.81
Radius of gyration Rg (electron density) rg_electron45.26
Forward intensity I(0) i0738432000.00
Molecular weight molecular_weight226750.0 kDa
Excluded volume excluded_volume285240 ų
Envelope volume envelope_volume415500 ų
Hydration-shell volume shell_volume76612 ų
Envelope diameter envelope_diameter141.0
Shell Rg shell_rg50.47
Envelope Rg envelope_rg43.46
Shape Rg shape_rg45.24
Total Rg total_rg45.58
Total atoms total_atoms15926
Residues n_residues1996
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 dmax146.4
Rg (real space) rg_real45.57
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real7.3840e+08
I(0) uncertainty (real space) i0_real_error1.3600e+07
Rg (reciprocal space) rg_reciprocal45.81
I(0) (reciprocal space) i0_reciprocal738600000.0000
Solution quality estimate total_estimate0.8979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.3
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.579
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63460000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)