Research workbench
AlphaFold monomer V2.0 prediction for GTPase obg (B1ZL15)
Analyse AlphaFold monomer V2.0 prediction for GTPase obg (B1ZL15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1ZL15
- Type
- protein
- Length
- 344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7627501bA56CC95b4fadf15f9A6c07FbB6e86a05
- Molecule
- GTPase obg
- UniProt
- B1ZL15
- Pockets
- 4 · best druggability 0.57
Structure
1 distinct chain · 24% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase obg | protein | 344 | 24% helix, 24% strand | B1ZL15 |
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 | 229 | 0.57 | 0.79 | 34 | empty |
| 2 | 110 | 0.55 | 0.84 | 30 | empty |
| 3 | 70 | 0.52 | 0.85 | 16 | empty |
| 4 | 95 | 0.38 | 0.76 | 12 | 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 B1ZL15
- Elsewhere: UniProt B1ZL15 · AlphaFold DB B1ZL15
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