MolNFT v1 · #171102 · protein
CLK1 bound with benzothiazole TG003 (cpd 2)
6YTE · Dual specificity protein kinase CLK1: “CLK1 bound with benzothiazole TG003 (cpd 2)”. X-ray diffraction, 1 ligand (EAE), 2 pockets (best druggability 0.70). MolNFT v1 #171102 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6YTE
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein kinase CLK1
- EC
- 2.7.12.1
- UniProt
- P49759
- Ligands
- EAE
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Dual specificity protein kinase CLK1 (EC 2.7.12.1) | protein | 338 | 40% helix, 20% strand | P49759 |
Ligands and binding sites
- EAE · (1~{Z})-1-(3-ethyl-5-methoxy-1,3-benzothiazol-2-ylidene)propan-2-one · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 349 | 0.70 | 0.82 | 46 | EAE |
| 2 | 59 | 0.32 | 0.76 | 11 | empty |
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 P49759
- Elsewhere: RCSB PDB 6YTE · PDBe 6YTE · UniProt P49759
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