Research workbench
Murine IFNAR1 in complex with interferon-beta
Analyse Murine IFNAR1 in complex with interferon-beta in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WCY
- Type
- protein
- Length
- 478 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon ALPHA/BETA receptor 1; Interferon beta
- UniProt
- P33896, P01575
- Pockets
- 10 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon ALPHA/BETA receptor 1 | protein | 318 | 3% helix, 39% strand | P33896 |
| I | Interferon beta | protein | 160 | 73% helix, 0% strand | P01575 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.61 | 0.79 | 45 | empty |
| 2 | 348 | 0.58 | 0.76 | 33 | empty |
| 3 | 245 | 0.57 | 0.78 | 22 | empty |
| 4 | 173 | 0.50 | 0.77 | 22 | empty |
| 5 | 114 | 0.45 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–I · 1694 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3WCY · Murine Ifnar1 in complex with interferon-beta · the same entry in another collection · chain A against A, TM-score 1.00
- P01575 · AlphaFold monomer V2.0 prediction for interferon beta (P01575) · a predicted model of the same protein · chain I against A, TM-score 0.97
- P33896 · AlphaFold monomer V2.0 prediction for interferon ALPHA/BETA receptor 1 (P33896) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P33896
- Every structure of UniProt P01575
- Elsewhere: RCSB PDB 3WCY · PDBe 3WCY · UniProt P33896 · UniProt P01575
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