MolNFT v1 · #62118 · protein
Fragment based discovery of JAK-2 inhibitors
3E64 · Tyrosine-protein kinase JAK2: “Fragment based discovery of JAK-2 inhibitors”. X-ray diffraction, 1 ligand (5B3), 2 pockets (best druggability 0.71). MolNFT v1 #62118 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3E64
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase JAK2
- EC
- 2.7.10.2
- UniProt
- O60674
- Ligands
- 5B3
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 293 | 44% helix, 19% strand | O60674 |
Ligands and binding sites
- 5B3 · 4-(3-amino-1H-indazol-5-yl)-N-tert-butylbenzenesulfonamide · ligand · chains A
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 | 570 | 0.71 | 0.80 | 60 | 5B3 |
| 2 | 51 | 0.27 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3E64 · Fragment based discovery of JAK-2 inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
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 O60674
- Elsewhere: RCSB PDB 3E64 · PDBe 3E64 · UniProt O60674
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