Research workbench
Structure of the LRRK2 monomer
Analyse Structure of the LRRK2 monomer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LHW
- Type
- protein
- Length
- 1,813 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine-rich repeat SERINE/THREONINE-protein kinase 2
- EC
- 2.7.11.1, 3.6.5.-
- UniProt
- Q5S007
- Ligands
- GDP, ATP
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 29% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine-rich repeat SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1, 3.6.5.-) | protein | 1813 | 29% helix, 16% strand | Q5S007 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1059 | 0.77 | 0.79 | 66 | empty |
| 2 | 549 | 0.77 | 0.84 | 70 | empty |
| 3 | 775 | 0.74 | 0.79 | 65 | empty |
| 4 | 478 | 0.70 | 0.80 | 51 | empty |
| 5 | 326 | 0.69 | 0.83 | 62 | empty |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q5S007
- Elsewhere: RCSB PDB 7LHW · PDBe 7LHW · UniProt Q5S007
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