Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIP12 (F1RCR6)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIP12… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- F1RCR6
- Type
- protein
- Length
- 2,026 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01a12c15Eab6FFCFA8a2083d486B834c1B47E8c8
- Molecule
- E3 ubiquitin-protein ligase TRIP12
- UniProt
- F1RCR6
- Pockets
- 20 · best druggability 0.79
Structure
1 distinct chain · 39% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase TRIP12 | protein | 2026 | 39% helix, 5% strand | F1RCR6 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 752 | 0.79 | 0.83 | 82 | empty |
| 2 | 610 | 0.78 | 0.84 | 61 | empty |
| 3 | 607 | 0.75 | 0.82 | 59 | empty |
| 4 | 288 | 0.70 | 0.85 | 34 | empty |
| 5 | 350 | 0.66 | 0.80 | 40 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 F1RCR6
- Elsewhere: UniProt F1RCR6 · AlphaFold DB F1RCR6
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