Research workbench
AlphaFold monomer V2.0 prediction for protein-glutamate METHYLESTERASE/PROTEIN-glutamine glutaminase (Q98PD1)
Analyse AlphaFold monomer V2.0 prediction for protein-glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q98PD1
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41f14059A2ce2B9bfD2DFE723f11dad3eCa2614e
- Molecule
- Protein-glutamate METHYLESTERASE/PROTEIN-glutamine glutaminase
- UniProt
- Q98PD1
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-glutamate METHYLESTERASE/PROTEIN-glutamine glutaminase | protein | 339 | 36% helix, 22% strand | Q98PD1 |
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 | 397 | 0.69 | 0.81 | 52 | empty |
| 2 | 293 | 0.61 | 0.78 | 34 | empty |
| 3 | 69 | 0.31 | 0.74 | 18 | 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 Q98PD1
- Elsewhere: UniProt Q98PD1 · AlphaFold DB Q98PD1
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