Research workbench
Crystal structure of TTBK1 in complex with VNG2.73 (compound 42)
Analyse Crystal structure of TTBK1 in complex with VNG2.73 (compound 42) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q8V
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tau-tubulin kinase 1
- EC
- 2.7.11.1
- UniProt
- Q5TCY1
- Ligands
- 9IV, PO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tau-tubulin kinase 1 (EC 2.7.11.1) | protein | 292 | 34% helix, 17% strand | Q5TCY1 |
Ligands and binding sites
- 9IV · ~{N}-[4-(2-chloranylphenoxy)phenyl]-7~{H}-pyrrolo[2,3-d]pyrimidin-4-amine · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 305 | 0.62 | 0.79 | 38 | 9IV |
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 Q5TCY1
- Elsewhere: RCSB PDB 7Q8V · PDBe 7Q8V · UniProt Q5TCY1
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