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TTBK1 in complex with ATP

Analyse TTBK1 in complex with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BTJ
Type
protein
Length
585 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tau-tubulin kinase 1
EC
2.7.11.1, 2.7.11.26
UniProt
Q5TCY1
Ligands
ADP, ATP, PO4
Pockets
4 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATau-tubulin kinase 1 (EC 2.7.11.1, 2.7.11.26)protein29234% helix, 17% strandQ5TCY1
BTau-tubulin kinase 1 (EC 2.7.11.1, 2.7.11.26)protein29335% helix, 18% strandQ5TCY1

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • ATP · Adenosine-5'-triphosphate · ligand · chains B
  • PO4 · Phosphate ion · ion · 4 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19760.740.77101ADP, PO4
22980.660.8239ATP
3530.310.7612empty
4610.290.7415empty

Interfaces

1 interface between chains.

  • A–B · 342 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 4BTJ · TTBK1 in complex with ATP · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5TCY1 · AlphaFold monomer V2.0 prediction for tau-tubulin kinase 1 (Q5TCY1) · a predicted model of the same protein · chain B against A, TM-score 0.99

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