Research workbench
Phosphorylation-dependent interaction between tumor suppressors dlg and lgl
Analyse Phosphorylation-dependent interaction between tumor suppressors dlg and lgl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WP1
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disks large homolog 4; LETHAL(2) giant larvae protein homolog 2
- UniProt
- P31016, Q6P1M3
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Disks large homolog 4 | protein | 180 | 43% helix, 21% strand | P31016 |
| A | LETHAL(2) giant larvae protein homolog 2 | protein | 12 | 42% helix, 0% strand | Q6P1M3 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.63 | 0.83 | 26 | empty |
| 2 | 100 | 0.40 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- B–A · 657 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3WP1 · Phosphorylation-dependent interaction between tumor suppressors Dlg and Lgl · the same entry in another collection · chain B against B, TM-score 1.00
- P31016 · AlphaFold monomer V2.0 prediction for disks large homolog 4 (P31016) · a predicted model of the same protein · chain B against A, TM-score 0.99
- 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 0.50
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 P31016
- Every structure of UniProt Q6P1M3
- Elsewhere: RCSB PDB 3WP1 · PDBe 3WP1 · UniProt P31016 · UniProt Q6P1M3
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