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The co-crystal structure of DYRK2 with yk-2-69

Analyse The co-crystal structure of DYRK2 with yk-2-69 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EJV
Type: protein
Length: 776 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q92630
Ligands: YK2

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	385	—	Q92630
B	—	protein	391	—	Q92630

Ligands and binding sites

YK2 · [6-[[4-[2-(dimethylamino)-1,3-benzothiazol-6-yl]-5-fluoranyl-pyrimidin-2-yl]amino]pyridin-3-yl]-(4-ethylpiperazin-1-yl)methanone · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

7EJV · The co-crystal structure of DYRK2 with YK-2-69 · the same entry in another collection · chain A against A, TM-score 1.00
Q92630 · AlphaFold monomer V2.0 prediction for dual specificity tyrosine… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q92630
Elsewhere: RCSB PDB 7EJV · PDBe 7EJV · UniProt Q92630

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