MolNFT v1 · #171440 · protein
Crystal structure of CLK3 in complex with macrocycle ODS2003178
6Z54: “Crystal structure of CLK3 in complex with macrocycle ODS2003178”. X-ray diffraction, 2 ligands (Q7H, PO4). MolNFT v1 #171440 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6Z54
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P49761
- Ligands
- Q7H, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 351 | — | P49761 |
Ligands and binding sites
- Q7H · 11,15-dimethyl-6-(oxan-4-yloxy)-8-oxa-2,11,15,19,21,23-hexazatetracyclo[15.6.1.13,7.020,24]pentacosa-1(23), 3(25),4,6,17,20(24),21-heptaen-10-one · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 13 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Z54 · Crystal structure of CLK3 in complex with macrocycle ODS2003178 · the same entry in another collection · chain A against A, TM-score 1.00
- P49761 · AlphaFold monomer V2.0 prediction for dual specificity protein kinase CLK3 (P49761) · a predicted model of the same protein · chain A 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 P49761
- Elsewhere: RCSB PDB 6Z54 · PDBe 6Z54 · UniProt P49761
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