Research workbench
AlphaFold monomer V2.0 prediction for bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme (B7MP27)
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
- B7MP27
- Type
- protein
- Length
- 890 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme
- UniProt
- B7MP27
- Pockets
- 12 · best druggability 0.71
Structure
1 distinct chain · 56% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional URIDYLYLTRANSFERASE/URIDYLYL-removing enzyme | protein | 890 | 56% helix, 11% strand | B7MP27 |
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.71 | 0.79 | 63 | empty |
| 2 | 508 | 0.69 | 0.79 | 61 | empty |
| 3 | 502 | 0.64 | 0.77 | 57 | empty |
| 4 | 220 | 0.59 | 0.80 | 34 | empty |
| 5 | 286 | 0.57 | 0.77 | 28 | 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 B7MP27
- Elsewhere: UniProt B7MP27 · AlphaFold DB B7MP27
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