Research workbench
AlphaFold monomer V2.0 prediction for gpi-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 (Q03515)
Analyse AlphaFold monomer V2.0 prediction for gpi-linked NAD(P)(+)--arginine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q03515
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Gpi-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1
- UniProt
- Q03515
- Pockets
- 4 · best druggability 0.63
Structure
1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gpi-linked NAD(P)(+)--arginine ADP-ribosyltransferase 1 | protein | 327 | 46% helix, 17% strand | Q03515 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.63 | 0.80 | 43 | empty |
| 2 | 189 | 0.53 | 0.78 | 27 | empty |
| 3 | 141 | 0.47 | 0.78 | 23 | empty |
| 4 | 113 | 0.45 | 0.78 | 20 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q03515
- Elsewhere: UniProt Q03515 · AlphaFold DB Q03515
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