MolNFT v1 · #127855 · protein
Crystal structure of human il-17AF
5N92 · Interleukin-17A: “Crystal structure of human il-17AF”. X-ray diffraction, 2 ligands (NAG, FUC), 3 pockets (best druggability 0.75). MolNFT v1 #127855 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5N92
- Type
- protein
- Length
- 229 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-17A; Interleukin-17F
- UniProt
- Q16552, Q96PD4
- Ligands
- NAG, FUC
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-17A | protein | 109 | 4% helix, 53% strand | Q16552 |
| F | Interleukin-17F | protein | 120 | 3% helix, 50% strand | Q96PD4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains F
- FUC · alpha-L-fucopyranose · sugar · chains F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.75 | 0.94 | 38 | empty |
| 2 | 201 | 0.50 | 0.76 | 26 | empty |
| 3 | 104 | 0.42 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–F · 2844 Ų buried · 49 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5N92 · Crystal Structure of Human IL-17AF · the same entry in another collection · chain A against A, TM-score 1.00
- 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
- Q96PD4 · AlphaFold monomer V2.0 prediction for interleukin-17F (Q96PD4) · a predicted model of the same protein · chain F against A, TM-score 0.77
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 Q96PD4
- Elsewhere: RCSB PDB 5N92 · PDBe 5N92 · UniProt Q16552 · UniProt Q96PD4
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