› 6xr4

Electron Microscopy
14Å resolution

Integrative in situ structure of Parkinsons disease-linked human LRRK2

Released:
DOI: 10.2210/pdb6xr4/pdb
PDB entry 6xr4 coloured by chain, ensemble of 53 models, front view.
PDB entry 6xr4 coloured by chain, ensemble of 53 models, side view.
PDB entry 6xr4 coloured by chain, ensemble of 53 models, top view.
Source organism: Homo sapiens
Primary publication:
The In Situ Structure of Parkinson's Disease-Linked LRRK2.
Watanabe R, Buschauer R, Böhning J, Audagnotto M, Lasker K, Lu TW, Boassa D, Taylor S, Villa E
Cell 182 1508-1518.e16 (2020)
PMID: 32783917
Related structures: EMD-20825

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine-rich repeat serine/threonine-protein kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 2527 amino acids
Theoretical weight: 286.45 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q5S007 (Residues: 1-2527; Coverage: 100%)
Gene names: LRRK2, PARK8
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 14Å
Relevant EMDB volumes: EMD-20825

Quick links

Citations

33 review citations

The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases.
Obsilova et al. (2020)
32 more

6 mentions without citation

An Update on the Interplay between LRRK2, Rab GTPases and Parkinson's Disease.
Komori et al. (2023)
5 more