MolNFT v1 · #165457 · protein
Re-refined crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole inhibitor
6TW2: “Re-refined crystal structure of di-phosphorylated human CLK1 in complex with a novel substituted indole…”. X-ray diffraction, 1 ligand (V25). MolNFT v1 #165457 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6TW2
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49759
- Ligands
- V25
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 334 | — | P49759 |
Ligands and binding sites
- V25 · ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylate · ligand · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TW2 · Re-refined crystal structure of di-phosphorylated human CLK1 in complex with a novel… · the same entry in another collection · chain E against E, TM-score 1.00
- P49759 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK1 (P49759) · a predicted model of the same protein · chain E against A, TM-score 0.97
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 6TW2 · PDBe 6TW2 · UniProt P49759
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