Research workbench
AlphaFold monomer V2.0 prediction for sialate O-acetylesterase (Q5RFU0)
Analyse AlphaFold monomer V2.0 prediction for sialate O-acetylesterase (Q5RFU0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RFU0
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6C7844EE9CCb104C5dBBCcd588586c47744E0fFf
- Molecule
- Sialate O-acetylesterase
- UniProt
- Q5RFU0
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 21% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sialate O-acetylesterase | protein | 523 | 21% helix, 27% strand | Q5RFU0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.50 | 0.80 | 24 | empty |
| 2 | 131 | 0.42 | 0.76 | 21 | empty |
| 3 | 50 | 0.27 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 5 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 Q5RFU0
- Elsewhere: UniProt Q5RFU0 · AlphaFold DB Q5RFU0
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