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DYRK1A in complex with XMD7-112

Analyse DYRK1A in complex with XMD7-112 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EJ4
Type: protein
Length: 1,345 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q13627
Ligands: B7W

Structure

x-ray diffraction · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	344	—	Q13627
B	—	protein	338	—	Q13627
C	—	protein	332	—	Q13627
D	—	protein	331	—	Q13627

Ligands and binding sites

B7W · 3-(3-pyridin-3-yl-1~{H}-pyrrolo[2,3-b]pyridin-5-yl) aniline · ligand · 4 copies · chains A, B, C, D

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

Compared structures

6EJ4 · DYRK1A in complex with XMD7-112 · the same entry in another collection · chain D against D, TM-score 1.00
Q13627 · 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 Q13627
Elsewhere: RCSB PDB 6EJ4 · PDBe 6EJ4 · UniProt Q13627

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