Research workbench
Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.
Analyse Crystal structure of the human cell polarity protein Lethal Giant Larvae 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N8P
- Type
- protein
- Length
- 827 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.193
- Source
- Homo sapiens
- Molecule
- Lethal(2) giant larvae protein homolog 2
- UniProt
- Q6P1M3
- Ligands
- CL
- Pockets
- 8 · best druggability 0.83
Structure
x-ray diffraction · resolution 3.193 · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lethal(2) giant larvae protein homolog 2 | protein | 827 | 6% helix, 47% strand | Q6P1M3 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.83 | 0.84 | 76 | CL |
| 2 | 1050 | 0.79 | 0.81 | 57 | empty |
| 3 | 247 | 0.67 | 0.84 | 28 | empty |
| 4 | 327 | 0.65 | 0.80 | 49 | empty |
| 5 | 54 | 0.41 | 0.82 | 18 | empty |
Compared structures
- 6N8P · Crystal structure of the human cell polarity protein lethal giant larvae 2 (LGL2).… · the same entry in another collection · chain A against A, TM-score 1.00
- Q6P1M3 · AlphaFold monomer V2.0 prediction for llgl scribble cell polarity complex component 2… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q6P1M3
- Elsewhere: RCSB PDB 6N8P · PDBe 6N8P · UniProt Q6P1M3
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