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The crystal structure of phosphorylated IRF-3
Analyse The crystal structure of phosphorylated IRF-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A77
- Type
- protein
- Length
- 929 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens
- Molecule
- Interferon regulatory factor 3
- UniProt
- Q14653
- Pockets
- 10 · best druggability 0.52
Structure
x-ray diffraction · resolution 1.8 · 4 distinct chains · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interferon regulatory factor 3 | protein | 232 | 27% helix, 30% strand | Q14653 |
| B | Interferon regulatory factor 3 | protein | 234 | 25% helix, 30% strand | Q14653 |
| C | Interferon regulatory factor 3 | protein | 233 | 27% helix, 30% strand | Q14653 |
| D | Interferon regulatory factor 3 | protein | 230 | 25% helix, 31% strand | Q14653 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains A, B, C, D
- ACY · Acetic acid · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.52 | 0.76 | 24 | empty |
| 2 | 246 | 0.52 | 0.76 | 24 | empty |
| 3 | 92 | 0.38 | 0.76 | 28 | empty |
| 4 | 53 | 0.35 | 0.79 | 18 | empty |
| 5 | 65 | 0.31 | 0.74 | 12 | empty |
Interfaces
5 interfaces between chains.
- A–B · 536 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 496 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 439 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 400 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 48 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 4 disulfide (phosphorylation, disulfide).
Compared structures
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 Q14653
- Elsewhere: RCSB PDB 3A77 · PDBe 3A77 · UniProt Q14653
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