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Crystal structure of il-17A/FAB6785 complex
Analyse Crystal structure of il-17A/FAB6785 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QHU
- Type
- protein
- Length
- 1,058 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAB6785 light chain; FAB6785 heavy chain; Interleukin-17A
- UniProt
- Q16552
- Ligands
- SO4, CL
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 5 distinct chains · 8% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, A | FAB6785 light chain | protein | 209 | 8% helix, 51% strand | — |
| H | FAB6785 heavy chain | protein | 211 | 9% helix, 51% strand | — |
| B | FAB6785 heavy chain | protein | 210 | 10% helix, 51% strand | — |
| C | Interleukin-17A | protein | 119 | 8% helix, 50% strand | Q16552 |
| D | Interleukin-17A | protein | 100 | 4% helix, 56% strand | Q16552 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains H, B, C, L, D
- CL · Chloride ion · ion · chains L
- GOL · Glycerol · additive · 5 copies · chains L, H, C, A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.82 | 0.96 | 40 | SO4 |
| 2 | 578 | 0.74 | 0.81 | 57 | GOL |
| 3 | 491 | 0.59 | 0.74 | 56 | empty |
| 4 | 369 | 0.54 | 0.73 | 44 | empty |
| 5 | 100 | 0.42 | 0.77 | 21 | empty |
Interfaces
9 interfaces between chains.
- C–D · 2731 Ų buried · 53 hydrogen bonds · protein-protein
- L–H · 1538 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1501 Ų buried · 11 hydrogen bonds · protein-protein
- L–C · 787 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 547 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide (disulfide).
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
- Elsewhere: RCSB PDB 4QHU · PDBe 4QHU · UniProt Q16552
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