MolNFT v1 · #110289 · protein
IRAK4-inhibitor co-structure
4XS2 · Interleukin-1 receptor-associated kinase 4: “IRAK4-inhibitor co-structure”. X-ray diffraction, 1 ligand (42P), 18 pockets (best druggability 0.83). MolNFT v1 #110289 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4XS2
- Type
- protein
- Length
- 1,131 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-1 receptor-associated kinase 4
- EC
- 2.7.11.1
- UniProt
- Q9NWZ3
- Ligands
- 42P
- Pockets
- 18 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-1 receptor-associated kinase 4 (EC 2.7.11.1) | protein | 286 | 41% helix, 16% strand | Q9NWZ3 |
| B | Interleukin-1 receptor-associated kinase 4 (EC 2.7.11.1) | protein | 281 | 41% helix, 15% strand | Q9NWZ3 |
| C | Interleukin-1 receptor-associated kinase 4 (EC 2.7.11.1) | protein | 284 | 42% helix, 17% strand | Q9NWZ3 |
| D | Interleukin-1 receptor-associated kinase 4 (EC 2.7.11.1) | protein | 280 | 41% helix, 17% strand | Q9NWZ3 |
Ligands and binding sites
- 42P · (1R,2S,3R,5R)-3-({5-(1,3-benzothiazol-2-yl)-6-chloro-2-[(3-methoxypropyl)amino]pyrimidin-4-yl}amino)-5-(hydroxymethyl)cyclopentane-1,2-diol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 618 | 0.83 | 0.88 | 85 | empty |
| 2 | 311 | 0.79 | 0.90 | 42 | empty |
| 3 | 812 | 0.74 | 0.79 | 57 | empty |
| 4 | 854 | 0.74 | 0.78 | 59 | empty |
| 5 | 51 | 0.71 | 0.99 | 21 | empty |
Interfaces
5 interfaces between chains.
- B–C · 653 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 645 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 644 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 572 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 304 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 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 Q9NWZ3
- Elsewhere: RCSB PDB 4XS2 · PDBe 4XS2 · UniProt Q9NWZ3
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