Research workbench
JAK3 kinase domain in complex with 2-cyclopropyl-5H-PYRROLO[2,3- B]PYRAZINE-7-carboxylic acid ((S)-2-hydroxy-1,2-dimethyl-propyl)- amide
Analyse JAK3 kinase domain in complex with 2-cyclopropyl-5H-PYRROLO[2,3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HVG
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase JAK3
- EC
- 2.7.10.2
- UniProt
- P52333
- Ligands
- 19Q
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK3 (EC 2.7.10.2) | protein | 281 | 44% helix, 21% strand | P52333 |
Ligands and binding sites
- 19Q · 2-cyclopropyl-N-[(2S)-3-hydroxy-3-methylbutan-2-yl]-5H-pyrrolo[2,3-b]pyrazine-7-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.73 | 0.98 | 18 | empty |
| 2 | 262 | 0.68 | 0.84 | 31 | 19Q |
| 3 | 180 | 0.55 | 0.80 | 32 | empty |
| 4 | 57 | 0.34 | 0.77 | 15 | empty |
Compared structures
- 4HVG · JAK3 kinase domain in complex with 2-Cyclopropyl-5H-pyrrolo[2,3-b]pyrazine-7-carboxylic… · the same entry in another collection · chain A against A, TM-score 1.00
- P52333 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase JAK3 (P52333) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P52333
- Elsewhere: RCSB PDB 4HVG · PDBe 4HVG · UniProt P52333
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