Research workbench
Il-27 quaternary receptor signaling complex
Analyse Il-27 quaternary receptor signaling complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7U7N
- Type
- protein
- Length
- 884 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-27 receptor subunit alpha; Interleukin-6 receptor subunit beta…
- UniProt
- Q6UWB1, P40189, Q14213, Q8NEV9
- Ligands
- NAG, BMA, MAN
- Pockets
- 9 · best druggability 0.72
Structure
electron microscopy · 4 distinct chains · 18% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-27 receptor subunit alpha | protein | 195 | 2% helix, 42% strand | Q6UWB1 |
| B | Interleukin-6 receptor subunit beta | protein | 298 | 8% helix, 44% strand | P40189 |
| C | Interleukin-27 subunit beta | protein | 200 | 2% helix, 51% strand | Q14213 |
| D | Interleukin-27 subunit alpha | protein | 191 | 68% helix, 1% strand | Q8NEV9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains B, C, A
- BMA · beta-D-mannopyranose · sugar · 3 copies
- MAN · alpha-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 663 | 0.72 | 0.79 | 74 | empty |
| 2 | 80 | 0.67 | 0.92 | 27 | empty |
| 3 | 225 | 0.65 | 0.84 | 39 | empty |
| 4 | 194 | 0.60 | 0.82 | 25 | empty |
| 5 | 175 | 0.57 | 0.81 | 25 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1438 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 863 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 726 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 472 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 343 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
- 7U7N · IL-27 quaternary receptor signaling complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q14213 · AlphaFold monomer V2.0 prediction for interleukin-27 subunit beta (Q14213) · a predicted model of the same protein · chain C against A, TM-score 0.97
- Q6UWB1 · AlphaFold monomer V2.0 prediction for interleukin-27 receptor subunit alpha (Q6UWB1) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P40189 · AlphaFold monomer V2.0 prediction for interleukin-6 receptor subunit beta (P40189) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q8NEV9 · AlphaFold monomer V2.0 prediction for interleukin-27 subunit alpha (Q8NEV9) · a predicted model of the same protein · chain D 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 Q6UWB1
- Every structure of UniProt P40189
- Every structure of UniProt Q14213
- Every structure of UniProt Q8NEV9
- Elsewhere: RCSB PDB 7U7N · PDBe 7U7N · UniProt Q6UWB1 · UniProt P40189 · UniProt Q14213 · UniProt Q8NEV9
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