Research workbench
Crystal structure of human il-10 complexed with the soluble il-10R1 chain
Analyse Crystal structure of human il-10 complexed with the soluble il-10R1 chain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y6K
- Type
- protein
- Length
- 350 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-10; Interleukin-10 receptor alpha chain
- UniProt
- P22301, Q13651
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Interleukin-10 | protein | 145 | 77% helix, 0% strand | P22301 |
| R | Interleukin-10 receptor alpha chain | protein | 205 | 7% helix, 46% strand | Q13651 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1167 | 0.72 | 0.75 | 76 | empty |
| 2 | 54 | 0.26 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- L–R · 861 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1Y6K · Crystal structure of human IL-10 complexed with the soluble IL-10R1 chain · the same entry in another collection · chain L against L, TM-score 1.00
- Q13651 · AlphaFold monomer V2.0 prediction for interleukin-10 receptor subunit alpha (Q13651) · a predicted model of the same protein · chain R against A, TM-score 0.99
- P22301 · AlphaFold monomer V2.0 prediction for interleukin-10 (P22301) · a predicted model of the same protein · chain L against A, TM-score 0.92
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 P22301
- Every structure of UniProt Q13651
- Elsewhere: RCSB PDB 1Y6K · PDBe 1Y6K · UniProt P22301 · UniProt Q13651
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