Research workbench
AlphaFold monomer V2.0 prediction for phosphoribosyl-dephospho-CoA transferase (Q89XP2)
Analyse AlphaFold monomer V2.0 prediction for phosphoribosyl-dephospho-CoA transferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q89XP2
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0Ee6C33B569Bce15FC75180A6ed0ae0a82F70934
- Molecule
- Phosphoribosyl-dephospho-CoA transferase
- UniProt
- Q89XP2
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosyl-dephospho-CoA transferase | protein | 226 | 33% helix, 24% strand | Q89XP2 |
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 | 286 | 0.56 | 0.77 | 32 | empty |
| 2 | 128 | 0.44 | 0.77 | 33 | empty |
| 3 | 58 | 0.26 | 0.72 | 14 | 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 Q89XP2
- Elsewhere: UniProt Q89XP2 · AlphaFold DB Q89XP2
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