Research workbench
DYRK1A in complex with fluoro benzothiazole fragment
Analyse DYRK1A in complex with fluoro benzothiazole fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A4L
- Type
- protein
- Length
- 1,350 residues
- Chains
- 4
- 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
- ZC3
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation- regulated kinase 1A (EC 2.7.12.1) | protein | 342 | 35% helix, 17% strand | Q13627 |
| B | Dual specificity tyrosine-phosphorylation- regulated kinase 1A (EC 2.7.12.1) | protein | 340 | 35% helix, 17% strand | Q13627 |
| C | Dual specificity tyrosine-phosphorylation- regulated kinase 1A (EC 2.7.12.1) | protein | 333 | 36% helix, 15% strand | Q13627 |
| D | Dual specificity tyrosine-phosphorylation- regulated kinase 1A (EC 2.7.12.1) | protein | 335 | 35% helix, 19% strand | Q13627 |
Ligands and binding sites
- ZC3 · N-(5-fluoranyl-1,3-benzothiazol-2-yl)ethanamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1000 | 0.84 | 0.84 | 99 | empty |
| 2 | 1172 | 0.83 | 0.84 | 118 | empty |
| 3 | 1037 | 0.79 | 0.80 | 96 | ZC3 |
| 4 | 1094 | 0.78 | 0.79 | 96 | ZC3 |
| 5 | 960 | 0.77 | 0.79 | 96 | ZC3 |
Interfaces
6 interfaces between chains.
- A–B · 1255 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1246 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 937 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 786 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 23 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 1 disulfide (phosphorylation, disulfide).
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 5A4L · PDBe 5A4L · UniProt Q13627
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.