Research workbench
Structure of interleukin-2 with its alpha receptor
Analyse Structure of interleukin-2 with its alpha receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z92
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-2; Interleukin-2 receptor alpha chain
- UniProt
- P60568, P01589
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-2 | protein | 121 | 63% helix, 3% strand | P60568 |
| B | Interleukin-2 receptor alpha chain | protein | 123 | 0% helix, 37% strand | P01589 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.46 | 0.80 | 22 | empty |
| 2 | 108 | 0.35 | 0.73 | 23 | empty |
| 3 | 66 | 0.29 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1005 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1Z92 · structure of interleukin-2 with its alpha receptor · the same entry in another collection · chain A against A, TM-score 1.00
- P01589 · AlphaFold monomer V2.0 prediction for interleukin-2 receptor subunit alpha (P01589) · a predicted model of the same protein · chain B against A, TM-score 0.93
- P60568 · AlphaFold monomer V2.0 prediction for interleukin-2 (P60568) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P60568
- Every structure of UniProt P01589
- Elsewhere: RCSB PDB 1Z92 · PDBe 1Z92 · UniProt P60568 · UniProt P01589
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