MolNFT v1 · #104844 · protein
MST3 in complex with staurosporine
4QMY · SERINE/THREONINE-protein kinase 24: “MST3 in complex with staurosporine”. X-ray diffraction, 2 ligands (STU, CL), 1 pocket (best druggability 0.66). MolNFT v1 #104844 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QMY
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase 24
- EC
- 2.7.11.1
- UniProt
- Q9Y6E0
- Ligands
- STU, CL
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase 24 (EC 2.7.11.1) | protein | 288 | 40% helix, 19% strand | Q9Y6E0 |
Ligands and binding sites
- STU · Staurosporine · ligand · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 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 | 384 | 0.66 | 0.79 | 37 | STU |
Modifications
Observed in the structure: 1 modified (phosphorylation).
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 Q9Y6E0
- Elsewhere: RCSB PDB 4QMY · PDBe 4QMY · UniProt Q9Y6E0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.