MolNFT v1 · #70648 · protein
Structure of the il-10R2 common chain
3LQM · Interleukin-10 receptor subunit beta: “Structure of the il-10R2 common chain”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.40). MolNFT v1 #70648 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LQM
- Type
- protein
- Length
- 397 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-10 receptor subunit beta
- UniProt
- Q08334
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-10 receptor subunit beta | protein | 201 | 5% helix, 51% strand | Q08334 |
| B | Interleukin-10 receptor subunit beta | protein | 196 | 6% helix, 50% strand | Q08334 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.40 | 0.81 | 17 | empty |
| 2 | 130 | 0.37 | 0.73 | 31 | empty |
| 3 | 62 | 0.28 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 848 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q08334
- Elsewhere: RCSB PDB 3LQM · PDBe 3LQM · UniProt Q08334
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