Research workbench
GSK3BETA complex with N-(6-(3,4-dihydroxyphenyl)-1H-PYRAZOLO[3,4- B]PYRIDIN-3-YL)ACETAMIDE
Analyse GSK3BETA complex with N-(6-(3,4-dihydroxyphenyl)-1H-PYRAZOLO[3,4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OY4
- Type
- protein
- Length
- 753 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycogen synthase kinase-3 beta; Proto-oncogene FRAT1
- EC
- 2.7.11.26, 2.7.11.1
- UniProt
- P49841, Q92837
- Ligands
- B4K, SO4
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycogen synthase kinase-3 beta (EC 2.7.11.26, 2.7.11.1) | protein | 350 | 34% helix, 19% strand | P49841 |
| B | Glycogen synthase kinase-3 beta (EC 2.7.11.26, 2.7.11.1) | protein | 354 | 35% helix, 20% strand | P49841 |
| X | Proto-oncogene FRAT1 | protein | 25 | 84% helix, 0% strand | Q92837 |
| Y | Proto-oncogene FRAT1 | protein | 24 | 83% helix, 0% strand | Q92837 |
Ligands and binding sites
- B4K · ~{N}-[6-[3,4-bis(oxidanyl)phenyl]-1~{H}-pyrazolo[3,4-b]pyridin-3-yl]ethanamide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 794 | 0.73 | 0.78 | 70 | empty |
| 2 | 250 | 0.64 | 0.81 | 29 | B4K |
| 3 | 253 | 0.62 | 0.80 | 30 | B4K |
| 4 | 365 | 0.57 | 0.75 | 36 | empty |
| 5 | 58 | 0.44 | 0.83 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 885 Ų buried · 12 hydrogen bonds · protein-protein
- A–X · 823 Ų buried · 6 hydrogen bonds · protein-protein
- B–Y · 803 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 5OY4 · GSK3beta complex with N-(6-(3,4-dihydroxyphenyl)-1H-pyrazolo[3,4-b]pyridin-3-yl)acetamide · the same entry in another collection · chain A against A, TM-score 1.00
- Q92837 · AlphaFold monomer V2.0 prediction for proto-oncogene FRAT1 (Q92837) · a predicted model of the same protein · chain Y against A, TM-score 0.92
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 P49841
- Every structure of UniProt Q92837
- Elsewhere: RCSB PDB 5OY4 · PDBe 5OY4 · UniProt P49841 · UniProt Q92837
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