Research workbench
Cryo-EM structure of the C-terminal half of the PARKINSON'S disease- linked protein leucine rich repeat kinase 2 (LRRK2)
Analyse Cryo-EM structure of the C-terminal half of the PARKINSON'S disease- linked… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VP7
- Type
- protein
- Length
- 1,084 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
- Pockets
- 19 · best druggability 0.74
Structure
electron microscopy · 1 distinct chain · 30% helix, 28% 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 | 1084 | 30% helix, 28% strand | Q5S007 |
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.74 | 0.95 | 16 | empty |
| 2 | 931 | 0.74 | 0.77 | 53 | empty |
| 3 | 381 | 0.72 | 0.83 | 48 | empty |
| 4 | 588 | 0.70 | 0.79 | 58 | empty |
| 5 | 456 | 0.69 | 0.80 | 56 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 6VP7 · Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5S007 · AlphaFold monomer V2.0 prediction for leucine-rich repeat SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 6VP7 · PDBe 6VP7 · UniProt Q5S007
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.