MolNFT v1 · #140353 · protein
Crystal structure of kinase
5Y86 · Dual specificity tyrosine-phosphorylation-regulated kinase 3: “Crystal structure of kinase”. X-ray diffraction, 2 ligands (HRM, PO4), 3 pockets (best druggability 0.68). MolNFT v1 #140353 on GenesisL1: 3D structure, binding sites…
- PDB
- 5Y86
- Type
- protein
- Length
- 395 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity tyrosine-phosphorylation-regulated kinase 3
- EC
- 2.7.12.1
- UniProt
- O43781
- Ligands
- HRM, PO4
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity tyrosine-phosphorylation-regulated kinase 3 (EC 2.7.12.1) | protein | 395 | 35% helix, 18% strand | O43781 |
Ligands and binding sites
- HRM · 7-methoxy-1-methyl-9H-beta-carboline · ligand · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 436 | 0.68 | 0.80 | 50 | HRM, EDO |
| 2 | 71 | 0.36 | 0.77 | 13 | empty |
| 3 | 58 | 0.31 | 0.76 | 12 | EDO |
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 O43781
- Elsewhere: RCSB PDB 5Y86 · PDBe 5Y86 · UniProt O43781
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