MolNFT v1 · #127856 · protein
Ttk kinase domain in complex with tc-MPS1-12
5N93 · Dual specificity protein kinase ttk: “Ttk kinase domain in complex with tc-MPS1-12”. X-ray diffraction, 1 ligand (8QE), 2 pockets (best druggability 0.77). MolNFT v1 #127856 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5N93
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein kinase ttk
- EC
- 2.7.12.1
- UniProt
- P33981
- Ligands
- 8QE
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein kinase ttk (EC 2.7.12.1) | protein | 260 | 36% helix, 22% strand | P33981 |
Ligands and binding sites
- 8QE · 4-[[4-azanyl-6-(~{tert}-butylamino)-5-cyano-pyridin-2-yl]amino]benzamide · ligand · chains A
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 | 248 | 0.77 | 0.90 | 36 | 8QE |
| 2 | 67 | 0.31 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 5N93 · TTK kinase domain in complex with TC-Mps1-12 · 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 P33981
- Elsewhere: RCSB PDB 5N93 · PDBe 5N93 · UniProt P33981
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