Research workbench
Structure of interleukin 17A in complex with IL17RA receptor
Analyse Structure of interleukin 17A in complex with IL17RA receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HSA
- Type
- protein
- Length
- 965 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-17A; Interleukin-17 receptor a
- UniProt
- Q16552, Q96F46
- Ligands
- NAG, MAN, FUC
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-17A | protein | 104 | 0% helix, 58% strand | Q16552 |
| B, E | Interleukin-17A | protein | 109 | 0% helix, 55% strand | Q16552 |
| C | Interleukin-17 receptor a | protein | 272 | 8% helix, 46% strand | Q96F46 |
| D | Interleukin-17A | protein | 100 | 4% helix, 59% strand | Q16552 |
| F | Interleukin-17 receptor a | protein | 271 | 8% helix, 46% strand | Q96F46 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains C, F
- MAN · alpha-D-mannopyranose · sugar · 4 copies
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains C, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 789 | 0.78 | 0.82 | 92 | empty |
| 2 | 601 | 0.77 | 0.83 | 69 | empty |
| 3 | 159 | 0.74 | 0.91 | 32 | empty |
| 4 | 170 | 0.73 | 0.90 | 33 | empty |
| 5 | 549 | 0.68 | 0.77 | 55 | empty |
Interfaces
10 interfaces between chains.
- D–E · 2507 Ų buried · 46 hydrogen bonds · protein-protein
- A–B · 2464 Ų buried · 47 hydrogen bonds · protein-protein
- E–F · 1347 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 1336 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1076 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
- 4HSA · Structure of interleukin 17a in complex with il17ra receptor · the same entry in another collection · chain F against F, TM-score 1.00
- Q96F46 · AlphaFold monomer V2.0 prediction for interleukin-17 receptor a (Q96F46) · a predicted model of the same protein · chain C against A, TM-score 0.96
- Q16552 · AlphaFold monomer V2.0 prediction for interleukin-17A (Q16552) · a predicted model of the same protein · chain B against A, TM-score 0.84
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
- Elsewhere: RCSB PDB 4HSA · PDBe 4HSA · UniProt Q16552 · UniProt Q96F46
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