Research workbench
AlphaFold monomer V2.0 prediction for bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme (A1JP85)
Analyse AlphaFold monomer V2.0 prediction for bifunctional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1JP85
- Type
- protein
- Length
- 892 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBffB45F145B2d50C65C0bb99786dC601f6D606C0
- Molecule
- Bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme
- UniProt
- A1JP85
- Pockets
- 13 · best druggability 0.68
Structure
1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme | protein | 892 | 55% helix, 11% strand | A1JP85 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.68 | 0.78 | 53 | empty |
| 2 | 589 | 0.66 | 0.76 | 62 | empty |
| 3 | 483 | 0.65 | 0.77 | 37 | empty |
| 4 | 371 | 0.63 | 0.78 | 52 | empty |
| 5 | 296 | 0.61 | 0.79 | 40 | empty |
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 A1JP85
- Elsewhere: UniProt A1JP85 · AlphaFold DB A1JP85
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