Research workbench
Crystal structure of human il-17AF in complex with human il-17RA
Analyse Crystal structure of human il-17AF in complex with human il-17RA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NAN
- Type
- protein
- Length
- 972 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-17A; Interleukin-17 receptor a; Interleukin-17F
- UniProt
- Q16552, Q96F46, Q96PD4
- Ligands
- NAG, GAL
- Pockets
- 18 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-17A | protein | 100 | 4% helix, 57% strand | Q16552 |
| B, C | Interleukin-17 receptor a | protein | 271 | 5% helix, 44% strand | Q96F46 |
| D | Interleukin-17A | protein | 104 | 4% helix, 59% strand | Q16552 |
| E, F | Interleukin-17F | protein | 113 | 4% helix, 58% strand | Q96PD4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains F, B, C, E
- GAL · beta-D-galactopyranose · sugar · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.72 | 0.97 | 18 | empty |
| 2 | 93 | 0.65 | 0.90 | 30 | empty |
| 3 | 166 | 0.63 | 0.85 | 33 | empty |
| 4 | 212 | 0.62 | 0.82 | 40 | empty |
| 5 | 167 | 0.59 | 0.83 | 27 | empty |
Interfaces
7 interfaces between chains.
- D–E · 2703 Ų buried · 42 hydrogen bonds · protein-protein
- A–F · 2499 Ų buried · 34 hydrogen bonds · protein-protein
- C–E · 1497 Ų buried · 18 hydrogen bonds · protein-protein
- B–F · 1494 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1075 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 5NAN · Crystal Structure of human IL-17AF in complex with human IL-17RA · 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 B against A, TM-score 0.91
- Q96PD4 · AlphaFold monomer V2.0 prediction for interleukin-17F (Q96PD4) · a predicted model of the same protein · chain E against A, TM-score 0.82
- Q16552 · AlphaFold monomer V2.0 prediction for interleukin-17A (Q16552) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 Q96PD4
- Elsewhere: RCSB PDB 5NAN · PDBe 5NAN · UniProt Q16552 · UniProt Q96F46 · UniProt Q96PD4
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