Research workbench
Crystal structures of JAK1 and JAK2 inhibitor complexes
Analyse Crystal structures of JAK1 and JAK2 inhibitor complexes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FUP
- Type
- protein
- Length
- 575 residues
- Chains
- 2
- 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
- MI1
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 286 | 43% helix, 19% strand | O60674 |
| B | Tyrosine-protein kinase JAK2 (EC 2.7.10.2) | protein | 289 | 42% helix, 20% strand | O60674 |
Ligands and binding sites
- MI1 · 3-{(3R,4R)-4-methyl-3-[methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]piperidin-1-yl}-3-oxopropanenitrile · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 495 | 0.75 | 0.84 | 56 | MI1 |
| 2 | 587 | 0.68 | 0.77 | 51 | empty |
| 3 | 163 | 0.63 | 0.85 | 28 | MI1 |
| 4 | 98 | 0.60 | 0.87 | 25 | empty |
| 5 | 138 | 0.40 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 568 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
Compared structures
- 3FUP · Crystal structures of JAK1 and JAK2 inhibitor complexes · 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 3FUP · PDBe 3FUP · UniProt O60674
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