Research workbench
AlphaFold monomer V2.0 prediction for orotidine 5'-phosphate decarboxylase (B1XXP1)
Analyse AlphaFold monomer V2.0 prediction for orotidine 5'-phosphate decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1XXP1
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Orotidine 5'-phosphate decarboxylase
- UniProt
- B1XXP1
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Orotidine 5'-phosphate decarboxylase | protein | 284 | 49% helix, 18% strand | B1XXP1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.52 | 0.79 | 25 | empty |
| 2 | 103 | 0.42 | 0.77 | 18 | empty |
| 3 | 80 | 0.37 | 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 B1XXP1
- Elsewhere: UniProt B1XXP1 · AlphaFold DB B1XXP1
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