Research workbench
Structure of the pry-spry domain of human TRIM16L/TRIM70
Analyse Structure of the pry-spry domain of human TRIM16L/TRIM70 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SJH
- Type
- protein
- Length
- 561 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tripartite motif-containing protein 16-like protein
- UniProt
- Q309B1
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 5% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tripartite motif-containing protein 16-like protein | protein | 187 | 5% helix, 44% strand | Q309B1 |
| B | Tripartite motif-containing protein 16-like protein | protein | 185 | 4% helix, 44% strand | Q309B1 |
| C | Tripartite motif-containing protein 16-like protein | protein | 189 | 5% helix, 44% strand | Q309B1 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 586 | 0.70 | 0.79 | 51 | empty |
| 2 | 189 | 0.44 | 0.74 | 32 | empty |
| 3 | 102 | 0.37 | 0.74 | 23 | empty |
| 4 | 74 | 0.32 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 686 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 505 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 46 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6SJH · Structure of the PRY-SPRY domain of human Trim16L/Trim70 · the same entry in another collection · chain A against A, TM-score 1.00
- Q309B1 · AlphaFold monomer V2.0 prediction for tripartite motif-containing protein 16-like protein… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q309B1
- Elsewhere: RCSB PDB 6SJH · PDBe 6SJH · UniProt Q309B1
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