MolNFT v1 · #57939 · protein
Human DYRK1A/HARMINE complex
3ANR · Dual specificity tyrosine-phosphorylation-regulated kinase…: “Human DYRK1A/HARMINE complex”. X-ray diffraction, 1 ligand (HRM), 11 pockets (best druggability 0.85). MolNFT v1 #57939 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3ANR
- Type
- protein
- Length
- 1,365 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
- HRM
- Pockets
- 11 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 343 | 35% helix, 18% strand | Q13627 |
| B | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 343 | 36% helix, 18% strand | Q13627 |
| C | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 338 | 36% helix, 18% strand | Q13627 |
| D | Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) | protein | 341 | 35% helix, 18% strand | Q13627 |
Ligands and binding sites
- HRM · 7-methoxy-1-methyl-9H-beta-carboline · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1162 | 0.85 | 0.86 | 130 | empty |
| 2 | 1081 | 0.84 | 0.84 | 101 | empty |
| 3 | 819 | 0.78 | 0.82 | 86 | HRM |
| 4 | 868 | 0.78 | 0.81 | 97 | HRM |
| 5 | 710 | 0.78 | 0.82 | 90 | HRM |
Interfaces
6 interfaces between chains.
- A–B · 1260 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1228 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 821 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 788 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 61 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 3ANR · PDBe 3ANR · UniProt Q13627
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