Research workbench
Crystal structure of the interleukin-1 receptor antagonist
Analyse Crystal structure of the interleukin-1 receptor antagonist in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ILR
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-1 receptor antagonist protein
- UniProt
- P18510
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Interleukin-1 receptor antagonist protein | protein | 145 | 10% helix, 51% strand | P18510 |
| 2 | Interleukin-1 receptor antagonist protein | protein | 144 | 8% helix, 50% strand | P18510 |
Interfaces
1 interface between chains.
- 1–2 · 624 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1ILR · Crystal structure of the interleukin-1 receptor antagonist · the same entry in another collection · chain 1 against 1, TM-score 1.00
- P18510 · AlphaFold monomer V2.0 prediction for interleukin-1 receptor antagonist protein (P18510) · a predicted model of the same protein · chain 1 against A, TM-score 0.98
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 P18510
- Elsewhere: RCSB PDB 1ILR · PDBe 1ILR · UniProt P18510
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