Research workbench
Crystal structure of the horse mlkl pseudokinase domain
Analyse Crystal structure of the horse mlkl pseudokinase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VC0
- Type
- protein
- Length
- 812 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mixed lineage kinase domain like pseudokinase
- UniProt
- F6S337
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mixed lineage kinase domain like pseudokinase | protein | 272 | 39% helix, 17% strand | F6S337 |
| B | Mixed lineage kinase domain like pseudokinase | protein | 269 | 41% helix, 17% strand | F6S337 |
| C | Mixed lineage kinase domain like pseudokinase | protein | 271 | 42% helix, 17% strand | F6S337 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.78 | 0.80 | 100 | GOL |
| 2 | 456 | 0.75 | 0.84 | 57 | empty |
| 3 | 119 | 0.65 | 0.88 | 20 | empty |
| 4 | 124 | 0.47 | 0.79 | 30 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1414 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1227 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6VC0 · Crystal structure of the horse MLKL pseudokinase domain · the same entry in another collection · chain A against A, TM-score 1.00
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 F6S337
- Elsewhere: RCSB PDB 6VC0 · PDBe 6VC0 · UniProt F6S337
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