Research workbench
Inter-molecular interactions in a 44 kda interferon-receptor complex detected by asymmetric back-protonation and 2D noesy
Analyse Inter-molecular interactions in a 44 kda interferon-receptor complex detected… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KZ1
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interferon alpha-2; Soluble ifn ALPHA/BETA receptor
- UniProt
- P01563, Q15467
- Pockets
- 4 · best druggability 0.79
Structure
solution nmr · 2 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon alpha-2 | protein | 165 | 61% helix, 0% strand | P01563 |
| B | Soluble ifn ALPHA/BETA receptor | protein | 196 | 2% helix, 46% strand | Q15467 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.79 | 0.84 | 55 | empty |
| 2 | 125 | 0.70 | 0.91 | 29 | empty |
| 3 | 162 | 0.44 | 0.75 | 21 | empty |
| 4 | 72 | 0.31 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1594 Ų buried · 31 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 2KZ1 · Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by… · the same entry in another collection · chain A against A, TM-score 1.00
- P01563 · AlphaFold monomer V2.0 prediction for interferon alpha-2 (P01563) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 P01563
- Every structure of UniProt Q15467
- Elsewhere: RCSB PDB 2KZ1 · PDBe 2KZ1 · UniProt P01563 · UniProt Q15467
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