Research workbench
Structure of the il-17A-il-17RA-il-17RC ternary complex
Analyse Structure of the il-17A-il-17RA-il-17RC ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UWN
- Type
- protein
- Length
- 1,325 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-17A; Interleukin-17 receptor a; Isoform 5 of interleukin-17 receptor C
- UniProt
- Q16552, Q96F46, Q8NAC3
- Ligands
- NAG
- Pockets
- 19 · best druggability 0.77
Structure
electron microscopy · 7 distinct chains · 6% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-17A | protein | 111 | 4% helix, 52% strand | Q16552 |
| B | Interleukin-17A | protein | 111 | 0% helix, 42% strand | Q16552 |
| C | Interleukin-17 receptor a | protein | 264 | 8% helix, 38% strand | Q96F46 |
| D | Interleukin-17A | protein | 106 | 3% helix, 55% strand | Q16552 |
| E | Interleukin-17A | protein | 93 | 0% helix, 55% strand | Q16552 |
| F | Interleukin-17 receptor a | protein | 237 | 7% helix, 35% strand | Q96F46 |
| G | Isoform 5 of interleukin-17 receptor C | protein | 403 | 9% helix, 44% strand | Q8NAC3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 11 copies · chains C, A, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.77 | 0.91 | 33 | empty |
| 2 | 611 | 0.74 | 0.81 | 73 | empty |
| 3 | 490 | 0.74 | 0.83 | 70 | empty |
| 4 | 349 | 0.72 | 0.84 | 49 | empty |
| 5 | 89 | 0.67 | 0.92 | 28 | empty |
Interfaces
9 interfaces between chains.
- A–B · 2581 Ų buried · 38 hydrogen bonds · protein-protein
- D–E · 2346 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 1443 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1403 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1213 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 disulfide, 10 glycan (disulfide, N-glycosylation).
Compared structures
- 7UWN · Structure of the IL-17A-IL-17RA-IL-17RC ternary complex · the same entry in another collection · chain G against G, TM-score 1.00
- Q96F46 · AlphaFold monomer V2.0 prediction for interleukin-17 receptor a (Q96F46) · a predicted model of the same protein · chain F against A, TM-score 0.97
- Q8NAC3 · AlphaFold monomer V2.0 prediction for interleukin-17 receptor C (Q8NAC3) · a predicted model of the same protein · chain G against A, TM-score 0.91
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 Q16552
- Every structure of UniProt Q96F46
- Every structure of UniProt Q8NAC3
- Elsewhere: RCSB PDB 7UWN · PDBe 7UWN · UniProt Q16552 · UniProt Q96F46 · UniProt Q8NAC3
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