MolNFT v1 · #113542 · protein
Human DYRK1A in complex with ldn-211898
5AIK · DYRK1A dual-specificity tyrosine-phosphorylation regulated…: “Human DYRK1A in complex with ldn-211898”. X-ray diffraction, 2 ligands (AWR, PO4), 15 pockets (best druggability 0.84). MolNFT v1 #113542 on GenesisL1: 3D structure…
- PDB
- 5AIK
- Type
- protein
- Length
- 1,374 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DYRK1A dual-specificity tyrosine-phosphorylation regulated kinase 1A
- EC
- 2.7.11.1
- UniProt
- Q13627
- Ligands
- AWR, PO4
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DYRK1A dual-specificity tyrosine-phosphorylation regulated kinase 1A (EC 2.7.11.1) | protein | 345 | 36% helix, 18% strand | Q13627 |
| B, C | DYRK1A dual-specificity tyrosine-phosphorylation regulated kinase 1A (EC 2.7.11.1) | protein | 343 | 35% helix, 18% strand | Q13627 |
| D | DYRK1A dual-specificity tyrosine-phosphorylation regulated kinase 1A (EC 2.7.11.1) | protein | 343 | 36% helix, 18% strand | Q13627 |
Ligands and binding sites
- AWR · 4-(7-METHOXY-1-(TRIFLUOROMETHYL)-9H-PYRIDO[3,4-B]INDOL-9-yl)butan-1-amine · ligand · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 10 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1064 | 0.84 | 0.85 | 93 | empty |
| 2 | 931 | 0.78 | 0.80 | 84 | AWR, PO4 |
| 3 | 1075 | 0.77 | 0.79 | 91 | AWR, PO4 |
| 4 | 339 | 0.65 | 0.80 | 32 | AWR |
| 5 | 282 | 0.62 | 0.80 | 31 | AWR |
Interfaces
4 interfaces between chains.
- A–D · 1044 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 758 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 591 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 43 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 5AIK · PDBe 5AIK · UniProt Q13627
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