Research workbench
Human STK10 bound to dovitinib
Analyse Human STK10 bound to dovitinib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OWQ
- Type
- protein
- Length
- 509 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase 10
- EC
- 2.7.11.1
- UniProt
- O94804
- Ligands
- 38O
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase 10 (EC 2.7.11.1) | protein | 255 | 42% helix, 16% strand | O94804 |
| B | SERINE/THREONINE-protein kinase 10 (EC 2.7.11.1) | protein | 254 | 42% helix, 16% strand | O94804 |
Ligands and binding sites
- 38O · 4-amino-5-fluoro-3-[5-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]quinolin-2(1H)-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.66 | 0.79 | 48 | 38O |
| 2 | 395 | 0.66 | 0.79 | 44 | 38O |
| 3 | 114 | 0.35 | 0.73 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1422 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 O94804
- Elsewhere: RCSB PDB 5OWQ · PDBe 5OWQ · UniProt O94804
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