Research workbench
Pry-spry domain of TRIM25
Analyse Pry-spry domain of TRIM25 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B8E
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 UBIQUITIN/ISG15 ligase TRIM25
- EC
- 6.3.2.19, 6.3.2.-
- UniProt
- Q61510
- Ligands
- CL
- Pockets
- 3 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 UBIQUITIN/ISG15 ligase TRIM25 (EC 6.3.2.19, 6.3.2.-) | protein | 194 | 10% helix, 43% strand | Q61510 |
| B | E3 UBIQUITIN/ISG15 ligase TRIM25 (EC 6.3.2.19, 6.3.2.-) | protein | 192 | 11% helix, 43% strand | Q61510 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 89 | 0.41 | 0.78 | 18 | CL |
| 2 | 83 | 0.32 | 0.74 | 22 | empty |
| 3 | 77 | 0.28 | 0.72 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 314 Ų buried · 3 hydrogen bonds · protein-protein
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 Q61510
- Elsewhere: RCSB PDB 4B8E · PDBe 4B8E · UniProt Q61510
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