Research workbench
Interleukin-4 / receptor alpha chain complex
Analyse Interleukin-4 / receptor alpha chain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IAR
- Type
- protein
- Length
- 317 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (interleukin-4); Protein (interleukin-4 receptor alpha chain)
- UniProt
- P05112, P24394
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (interleukin-4) | protein | 129 | 63% helix, 5% strand | P05112 |
| B | Protein (interleukin-4 receptor alpha chain) | protein | 188 | 7% helix, 49% strand | P24394 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 167 | 0.48 | 0.77 | 22 | empty |
| 2 | 64 | 0.36 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 817 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1IAR · Interleukin-4 / receptor alpha chain complex · the same entry in another collection · chain A against A, TM-score 1.00
- P24394 · AlphaFold monomer V2.0 prediction for interleukin-4 receptor subunit alpha (P24394) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P05112 · AlphaFold monomer V2.0 prediction for interleukin-4 (P05112) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P05112
- Every structure of UniProt P24394
- Elsewhere: RCSB PDB 1IAR · PDBe 1IAR · UniProt P05112 · UniProt P24394
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