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Structure of the TIE2 kinase domain in complex with a thiazolopyrimidine inhibitor
Analyse Structure of the TIE2 kinase domain in complex with a thiazolopyrimidine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WQB
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Angiopoietin-1 receptor
- EC
- 2.7.10.1
- UniProt
- Q02763
- Ligands
- QQ1
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Angiopoietin-1 receptor (EC 2.7.10.1) | protein | 289 | 36% helix, 21% strand | Q02763 |
Ligands and binding sites
- QQ1 · 2-[3-(cyclohexylmethyl)-5-phenyl-imidazol-4-yl]-[1,3]thiazolo[4,5-e]pyrimidin-7-amine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.52 | 0.75 | 26 | QQ1 |
| 2 | 101 | 0.44 | 0.78 | 28 | empty |
| 3 | 50 | 0.38 | 0.81 | 22 | empty |
| 4 | 50 | 0.28 | 0.75 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2WQB · Structure of the Tie2 kinase domain in complex with a thiazolopyrimidine inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q02763 · AlphaFold monomer V2.0 prediction for angiopoietin-1 receptor (Q02763) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q02763
- Elsewhere: RCSB PDB 2WQB · PDBe 2WQB · UniProt Q02763
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