Research workbench
Structural and thermodynamic characterization of the TYK2 and JAK3 kinase domains in complex with cp-690550 and cmp-6
Analyse Structural and thermodynamic characterization of the TYK2 and JAK3 kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LXN
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non-receptor tyrosine-protein kinase TYK2
- EC
- 2.7.10.2
- UniProt
- P29597
- Ligands
- MI1
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Non-receptor tyrosine-protein kinase TYK2 (EC 2.7.10.2) | protein | 288 | 44% helix, 22% strand | P29597 |
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 · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.67 | 0.81 | 46 | MI1 |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3LXN · Structural and Thermodynamic Characterization of the TYK2 and JAK3 Kinase Domains in… · the same entry in another collection · chain A against A, TM-score 1.00
- P29597 · AlphaFold monomer V2.0 prediction for non-receptor tyrosine-protein kinase TYK2 (P29597) · 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 P29597
- Elsewhere: RCSB PDB 3LXN · PDBe 3LXN · UniProt P29597
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