MolNFT v1 · #171105 · protein
CLK1 bound with ETH1610 (cpd 17)
6YTI · Dual specificity protein kinase CLK1: “CLK1 bound with ETH1610 (cpd 17)”. X-ray diffraction, 1 ligand (7A7), 1 pocket (best druggability 0.67). MolNFT v1 #171105 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YTI
- Type
- protein
- Length
- 329 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
- 7A7
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein kinase CLK1 (EC 2.7.12.1) | protein | 329 | 40% helix, 18% strand | P49759 |
Ligands and binding sites
- 7A7 · Methyl 9-[(2-fluoranyl-4-methoxy-phenyl)amino]-[1, 3]thiazolo[5,4-f]quinazoline-2-carboximidate · ligand · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · 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 | 385 | 0.67 | 0.80 | 47 | EDO, 7A7 |
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 6YTI · PDBe 6YTI · UniProt P49759
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