Research workbench
AlphaFold monomer V2.0 prediction for multiphosphoryl transfer protein (P23388)
Analyse AlphaFold monomer V2.0 prediction for multiphosphoryl transfer protein (P23388) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23388
- Type
- protein
- Length
- 827 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Multiphosphoryl transfer protein
- UniProt
- P23388
- Pockets
- 6 · best druggability 0.82
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiphosphoryl transfer protein | protein | 827 | 47% helix, 18% strand | P23388 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 959 | 0.82 | 0.83 | 111 | empty |
| 2 | 184 | 0.68 | 0.87 | 28 | empty |
| 3 | 299 | 0.59 | 0.78 | 30 | empty |
| 4 | 67 | 0.30 | 0.75 | 15 | empty |
| 5 | 54 | 0.29 | 0.76 | 17 | 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 P23388
- Elsewhere: UniProt P23388 · AlphaFold DB P23388
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