8fo2

Cryo-EM structure of Rab29-LRRK2 complex in the LRRK2 monomer state

Method: ELECTRON MICROSCOPY Dmax: 214.3 Å Quality: GOOD

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

Ras-related protein Rab-7L1

Homo sapiens

UniProt O14966

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 B; UniProt 1–177 Not recorded Leucine-rich repeat serine/threonine-protein kinase 2 × 1 (Q5S007) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAB7L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–177; UniProt 1–177

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–2527 Not recorded Ras-related protein Rab-7L1 × 1 (O14966) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.13 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 E; PDBConstruct 1–2527; 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 8fo2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fo2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fo2
Deposition date deposition_date2022-12-29
最后修订 last_revision2024-01-03
Structure title titleCryo-EM structure of Rab29-LRRK2 complex in the LRRK2 monomer state
Keywords keywords;Cryo-EM, Parkinson's disease, Kinase, LRRK2, Rab GTPases, Activation, HYDROLASE ;; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.46
Radius of gyration Rg (electron density) rg_electron66.59
Forward intensity I(0) i0930821000.00
Molecular weight molecular_weight259800.0 kDa
Excluded volume excluded_volume327000 ų
Envelope volume envelope_volume533270 ų
Hydration-shell volume shell_volume72890 ų
Envelope diameter envelope_diameter235.8
Shell Rg shell_rg57.96
Envelope Rg envelope_rg66.50
Shape Rg shape_rg66.67
Total Rg total_rg66.10
Total atoms total_atoms18255
Residues n_residues2447
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 dmax214.3
Rg (real space) rg_real66.74
Rg uncertainty (real space) rg_real_error2.27
I(0) (real space) i0_real9.3060e+08
I(0) uncertainty (real space) i0_real_error2.1440e+07
Rg (reciprocal space) rg_reciprocal64.25
I(0) (reciprocal space) i0_reciprocal926600000.0000
Solution quality estimate total_estimate0.7561
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.557
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha41950000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.701; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.715; Smooth: 0.010

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)