MolNFT v1 · #189008 · protein
Structure of the il-17A-il-17RA binary complex
7UWM · Interleukin-17A: “Structure of the il-17A-il-17RA binary complex”. Electron microscopy, 1 ligand (NAG), 15 pockets (best druggability 0.77). MolNFT v1 #189008 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7UWM
- Type
- protein
- Length
- 967 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-17A; Interleukin-17 receptor a
- UniProt
- Q16552, Q96F46
- Ligands
- NAG
- Pockets
- 15 · best druggability 0.77
Structure
electron microscopy · 4 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Interleukin-17A | protein | 109 | 4% helix, 56% strand | Q16552 |
| B, E | Interleukin-17A | protein | 109 | 0% helix, 55% strand | Q16552 |
| C | Interleukin-17 receptor a | protein | 269 | 8% helix, 42% strand | Q96F46 |
| F | Interleukin-17 receptor a | protein | 262 | 8% helix, 44% strand | Q96F46 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains C, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 569 | 0.77 | 0.83 | 73 | empty |
| 2 | 172 | 0.74 | 0.91 | 33 | empty |
| 3 | 152 | 0.73 | 0.92 | 36 | empty |
| 4 | 288 | 0.73 | 0.86 | 34 | empty |
| 5 | 68 | 0.73 | 0.97 | 18 | empty |
Interfaces
7 interfaces between chains.
- D–E · 2482 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 2454 Ų buried · 44 hydrogen bonds · protein-protein
- B–C · 1457 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 1410 Ų buried · 22 hydrogen bonds · protein-protein
- D–F · 1164 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 disulfide, 8 glycan (disulfide, N-glycosylation).
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 Q16552
- Every structure of UniProt Q96F46
- Elsewhere: RCSB PDB 7UWM · PDBe 7UWM · UniProt Q16552 · UniProt Q96F46
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