Research workbench
Crystal structure of the il-22/IL-22R1 complex
Analyse Crystal structure of the il-22/IL-22R1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DLQ
- Type
- protein
- Length
- 332 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-22; Interleukin-22 receptor subunit alpha-1
- UniProt
- Q9GZX6, Q8N6P7
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I | Interleukin-22 | protein | 131 | 73% helix, 0% strand | Q9GZX6 |
| R | Interleukin-22 receptor subunit alpha-1 | protein | 201 | 8% helix, 48% strand | Q8N6P7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.60 | 0.80 | 29 | empty |
| 2 | 141 | 0.51 | 0.80 | 27 | empty |
| 3 | 70 | 0.35 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- I–R · 913 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3DLQ · Crystal structure of the IL-22/IL-22R1 complex · the same entry in another collection · chain I against I, TM-score 1.00
- Q9GZX6 · AlphaFold monomer V2.0 prediction for interleukin-22 (Q9GZX6) · a predicted model of the same protein · chain I against A, TM-score 0.99
- Q8N6P7 · AlphaFold monomer V2.0 prediction for interleukin-22 receptor subunit alpha-1 (Q8N6P7) · a predicted model of the same protein · chain R against A, TM-score 0.99
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 Q9GZX6
- Every structure of UniProt Q8N6P7
- Elsewhere: RCSB PDB 3DLQ · PDBe 3DLQ · UniProt Q9GZX6 · UniProt Q8N6P7
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