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Crystal structure of dlk (kinase domain)
Analyse Crystal structure of dlk (kinase domain) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CEN
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase kinase kinase 12
- EC
- 2.7.11.25
- UniProt
- Q12852
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase kinase kinase 12 (EC 2.7.11.25) | protein | 281 | 46% helix, 16% strand | Q12852 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.62 | 0.88 | 21 | empty |
| 2 | 223 | 0.60 | 0.80 | 32 | empty |
| 3 | 128 | 0.50 | 0.80 | 20 | 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 Q12852
- Elsewhere: RCSB PDB 5CEN · PDBe 5CEN · UniProt Q12852
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