Research workbench
Crystal structure of a CYTOKINE/RECEPTOR complex
Analyse Crystal structure of a CYTOKINE/RECEPTOR complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I1R
- Type
- protein
- Length
- 468 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-6 receptor beta chain; Viral il-6
- UniProt
- P40189, Q98823
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-6 receptor beta chain | protein | 301 | 8% helix, 47% strand | P40189 |
| B | Viral il-6 | protein | 167 | 63% helix, 1% strand | Q98823 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.45 | 0.78 | 15 | empty |
| 2 | 101 | 0.43 | 0.78 | 19 | empty |
| 3 | 84 | 0.41 | 0.79 | 18 | empty |
| 4 | 55 | 0.25 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 648 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 P40189
- Every structure of UniProt Q98823
- Elsewhere: RCSB PDB 1I1R · PDBe 1I1R · UniProt P40189 · UniProt Q98823
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