MolNFT v1 · #154625 · protein
Crystal structure of CLK2 in complex with cx-4945
6KHE · Dual specificity protein kinase CLK2: “Crystal structure of CLK2 in complex with cx-4945”. X-ray diffraction, 1 ligand (3NG), 3 pockets (best druggability 0.64). MolNFT v1 #154625 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6KHE
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity protein kinase CLK2
- EC
- 2.7.12.1
- UniProt
- P49760
- Ligands
- 3NG
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity protein kinase CLK2 (EC 2.7.12.1) | protein | 342 | 37% helix, 21% strand | P49760 |
Ligands and binding sites
- 3NG · 5-[(3-chlorophenyl)amino]benzo[c][2,6]naphthyridine-8-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.64 | 0.81 | 25 | 3NG |
| 2 | 95 | 0.36 | 0.75 | 14 | empty |
| 3 | 62 | 0.30 | 0.75 | 19 | 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 P49760
- Elsewhere: RCSB PDB 6KHE · PDBe 6KHE · UniProt P49760
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