Research workbench
Crystal structure of the TAO2 kinase domain: activation and specifity of a STE20P MAP3K
Analyse Crystal structure of the TAO2 kinase domain: activation and specifity of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U5Q
- Type
- protein
- Length
- 618 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE protein kinase TAO2
- UniProt
- Q9JLS3
- Ligands
- CA
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE protein kinase TAO2 | protein | 309 | 45% helix, 18% strand | Q9JLS3 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 778 | 0.76 | 0.80 | 75 | empty |
| 2 | 272 | 0.70 | 0.84 | 32 | empty |
| 3 | 252 | 0.68 | 0.84 | 31 | empty |
| 4 | 107 | 0.39 | 0.75 | 21 | empty |
| 5 | 69 | 0.34 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 765 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 1U5Q · Crystal Structure of the TAO2 Kinase Domain: Activation and Specifity of a Ste20p MAP3K · the same entry in another collection · chain A against A, TM-score 1.00
- Q9JLS3 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase TAO2 (Q9JLS3) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9JLS3
- Elsewhere: RCSB PDB 1U5Q · PDBe 1U5Q · UniProt Q9JLS3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.