Research workbench
Interleukin-3 receptor complex
Analyse Interleukin-3 receptor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UV8
- Type
- protein
- Length
- 737 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-3 receptor subunit alpha; Interleukin-3
- UniProt
- P26951, P08700
- Ligands
- NAG, BMA, FUC
- Pockets
- 11 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-3 receptor subunit alpha | protein | 259 | 3% helix, 50% strand | P26951 |
| B | Interleukin-3 | protein | 105 | 64% helix, 0% strand | P08700 |
| G | Interleukin-3 receptor subunit alpha | protein | 265 | 3% helix, 49% strand | P26951 |
| I | Interleukin-3 | protein | 108 | 62% helix, 0% strand | P08700 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, G
- BMA · beta-D-mannopyranose · sugar · 3 copies
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, G
- GOL · Glycerol · additive · 3 copies · chains G, I
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 | 343 | 0.70 | 0.83 | 44 | empty |
| 2 | 331 | 0.67 | 0.82 | 37 | empty |
| 3 | 535 | 0.65 | 0.77 | 60 | empty |
| 4 | 446 | 0.59 | 0.75 | 54 | GOL |
| 5 | 184 | 0.45 | 0.74 | 19 | empty |
Interfaces
5 interfaces between chains.
- G–I · 1223 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1203 Ų buried · 21 hydrogen bonds · protein-protein
- A–I · 409 Ų buried · 8 hydrogen bonds · protein-protein
- B–G · 406 Ų buried · 10 hydrogen bonds · protein-protein
- B–I · 357 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 5UV8 · Interleukin-3 Receptor Complex · the same entry in another collection · chain I against I, TM-score 1.00
- P26951 · AlphaFold monomer V2.0 prediction for interleukin-3 receptor subunit alpha (P26951) · a predicted model of the same protein · chain G against A, TM-score 0.97
- P08700 · AlphaFold monomer V2.0 prediction for interleukin-3 (P08700) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P26951
- Every structure of UniProt P08700
- Elsewhere: RCSB PDB 5UV8 · PDBe 5UV8 · UniProt P26951 · UniProt P08700
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