MolNFT v1 · #184666 · protein
Crystal structure of human DYRK1A in complex with ARN25068
7OY6 · Dual specificity tyrosine-phosphorylation-regulated kinase…: “Crystal structure of human DYRK1A in complex with ARN25068”. X-ray diffraction, 1 ligand (39I), 2 pockets (best druggability 0.59). MolNFT v1 #184666 on GenesisL1: 3D…
- PDB
- 7OY6
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- EC
- 2.7.12.1
- UniProt
- Q13627
- Ligands
- 39I
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 343 | 35% helix, 18% strand | Q13627 |
Ligands and binding sites
- 39I · ~{N}4-(3-cyclopropyl-1~{H}-pyrazol-5-yl)-~{N}2-(phenylmethyl)thieno[3,2-d]pyrimidine-2,4-diamine · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.59 | 0.78 | 33 | 39I |
| 2 | 81 | 0.43 | 0.79 | 18 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
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 7OY6 · PDBe 7OY6 · UniProt Q13627
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