Research workbench
AlphaFold monomer V2.0 prediction for adenosylcobinamide-GDP ribazoletransferase (Q5PDU1)
Analyse AlphaFold monomer V2.0 prediction for adenosylcobinamide-GDP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5PDU1
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x30d872b97D5A8BBB2071246F96F833576bC307D1
- Molecule
- Adenosylcobinamide-GDP ribazoletransferase
- UniProt
- Q5PDU1
- Pockets
- 2 · best druggability 0.59
Structure
1 distinct chain · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosylcobinamide-GDP ribazoletransferase | protein | 247 | 77% helix, 1% strand | Q5PDU1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.59 | 0.87 | 23 | empty |
| 2 | 87 | 0.35 | 0.74 | 15 | 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 Q5PDU1
- Elsewhere: UniProt Q5PDU1 · AlphaFold DB Q5PDU1
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