6vp7

Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)

Method: ELECTRON MICROSCOPY Dmax: 140.1 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1327–2527 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1201; UniProt 1327–2527

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 6vp7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vp7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vp7
Deposition date deposition_date2020-02-01
Structure title titleCryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)
Keywords keywordsKinase, GTPase, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.85
Radius of gyration Rg (electron density) rg_electron40.99
Forward intensity I(0) i018854900000.00
Molecular weight molecular_weight1213300.0 kDa
Excluded volume excluded_volume1534900 ų
Envelope volume envelope_volume218600 ų
Hydration-shell volume shell_volume47372 ų
Envelope diameter envelope_diameter141.6
Shell Rg shell_rg43.40
Envelope Rg envelope_rg40.04
Shape Rg shape_rg40.95
Total Rg total_rg41.16
Total atoms total_atoms85310
Residues n_residues10830
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 dmax140.1
Rg (real space) rg_real41.10
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real1.8850e+10
I(0) uncertainty (real space) i0_real_error3.3330e+08
Rg (reciprocal space) rg_reciprocal40.86
I(0) (reciprocal space) i0_reciprocal18850000000.0000
Solution quality estimate total_estimate0.7827
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.465
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27740000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.752; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6vp7A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id6vp7A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id6vp7A03
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)