Research workbench
AlphaFold monomer V2.0 prediction for multiphosphoryl transfer protein 2 (P32670)
Analyse AlphaFold monomer V2.0 prediction for multiphosphoryl transfer protein 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P32670
- Type
- protein
- Length
- 833 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Multiphosphoryl transfer protein 2
- UniProt
- P32670
- Pockets
- 9 · best druggability 0.74
Structure
1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiphosphoryl transfer protein 2 | protein | 833 | 48% helix, 17% strand | P32670 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.74 | 0.82 | 59 | empty |
| 2 | 117 | 0.69 | 0.91 | 25 | empty |
| 3 | 435 | 0.68 | 0.80 | 49 | empty |
| 4 | 122 | 0.52 | 0.81 | 29 | empty |
| 5 | 144 | 0.47 | 0.77 | 22 | 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 P32670
- Elsewhere: UniProt P32670 · AlphaFold DB P32670
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