Research workbench
AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase (P0AG16)
Analyse AlphaFold monomer V2.0 prediction for amidophosphoribosyltransferase (P0AG16) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AG16
- Type
- protein
- Length
- 505 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfD2aa30896c43ba48ACc736586610789048c2c7a
- Molecule
- Amidophosphoribosyltransferase
- UniProt
- P0AG16
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amidophosphoribosyltransferase | protein | 505 | 36% helix, 23% strand | P0AG16 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1109 | 0.80 | 0.81 | 77 | empty |
| 2 | 357 | 0.59 | 0.77 | 40 | empty |
| 3 | 86 | 0.35 | 0.75 | 20 | empty |
Compared structures
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 P0AG16
- Elsewhere: UniProt P0AG16 · AlphaFold DB P0AG16
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