Research workbench
Structure of MLKL
Analyse Structure of MLKL in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BTF
- Type
- protein
- Length
- 413 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.604
- Source
- MUS MUSCULUS
- Molecule
- Mixed lineage kinase domain-like protein
- UniProt
- Q9D2Y4
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · resolution 2.604 · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mixed lineage kinase domain-like protein | protein | 413 | 53% helix, 12% strand | Q9D2Y4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 411 | 0.62 | 0.77 | 41 | empty |
| 2 | 245 | 0.48 | 0.74 | 34 | empty |
| 3 | 122 | 0.48 | 0.79 | 26 | empty |
| 4 | 80 | 0.37 | 0.76 | 14 | empty |
| 5 | 54 | 0.31 | 0.76 | 15 | 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 Q9D2Y4
- Elsewhere: RCSB PDB 4BTF · PDBe 4BTF · UniProt Q9D2Y4
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