Research workbench
JAK1 kinase (JH1 domain) in complex with compound 30
Analyse JAK1 kinase (JH1 domain) in complex with compound 30 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E4L
- Type
- protein
- Length
- 1,125 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase JAK1
- EC
- 2.7.10.2
- UniProt
- P23458
- Ligands
- 0NH
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) | protein | 279 | 43% helix, 20% strand | P23458 |
| B | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) | protein | 281 | 43% helix, 20% strand | P23458 |
| E | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) | protein | 282 | 43% helix, 20% strand | P23458 |
| D | Tyrosine-protein kinase JAK1 (EC 2.7.10.2) | protein | 283 | 42% helix, 20% strand | P23458 |
Ligands and binding sites
- 0NH · 1-[4-methyl-1-(methylsulfonyl)piperidin-4-yl]-1,6-dihydroimidazo[4,5-d]pyrrolo[2,3-b]pyridine · ligand · 4 copies · chains A, E, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 486 | 0.77 | 0.85 | 56 | 0NH |
| 2 | 497 | 0.77 | 0.85 | 53 | 0NH |
| 3 | 738 | 0.77 | 0.81 | 67 | empty |
| 4 | 568 | 0.76 | 0.83 | 65 | 0NH |
| 5 | 505 | 0.74 | 0.83 | 56 | 0NH |
Interfaces
4 interfaces between chains.
- A–B · 977 Ų buried · 16 hydrogen bonds · protein-protein
- E–D · 946 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 449 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 56 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 P23458
- Elsewhere: RCSB PDB 4E4L · PDBe 4E4L · UniProt P23458
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