Research workbench
Crystal structure of DCLK1-cter in complex with fmf-03-055-1
Analyse Crystal structure of DCLK1-cter in complex with fmf-03-055-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KX8
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O15075
- Ligands
- X8J
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 263 | — | O15075 |
| B | — | protein | 251 | — | O15075 |
Ligands and binding sites
- X8J · 5-ethyl-2-{[2-methoxy-4-(4-methylpiperazin-1-yl) phenyl]amino}-11-methyl-5,11-dihydro-6H-pyrimido[4,5-b][1,4]benzodiazepin-6-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7KX8 · Crystal structure of DCLK1-Cter in complex with FMF-03-055-1 · the same entry in another collection · chain A against A, TM-score 1.00
- O15075 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase DCLK1 (O15075) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O15075
- Elsewhere: RCSB PDB 7KX8 · PDBe 7KX8 · UniProt O15075
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