Research workbench
AlphaFold monomer V2.0 prediction for GTPase obg (A1V0P1)
Analyse AlphaFold monomer V2.0 prediction for GTPase obg (A1V0P1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1V0P1
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x114a0357b11cFf6EBe7075749Ec3390CD780d178
- Molecule
- GTPase obg
- UniProt
- A1V0P1
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 26% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase obg | protein | 372 | 26% helix, 23% strand | A1V0P1 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.75 | 0.81 | 60 | empty |
| 2 | 154 | 0.56 | 0.81 | 20 | empty |
| 3 | 82 | 0.55 | 0.86 | 25 | empty |
| 4 | 78 | 0.33 | 0.75 | 11 | 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 A1V0P1
- Elsewhere: UniProt A1V0P1 · AlphaFold DB A1V0P1
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