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Sialidase from salmonella typhimurium
Analyse Sialidase from salmonella typhimurium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SIL
- Type
- protein
- Length
- 379 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.05
- Source
- Salmonella typhimurium
- Molecule
- Sialidase
- EC
- 3.2.1.18
- UniProt
- P29768
- Ligands
- K, PO4
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · resolution 1.05 · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sialidase (EC 3.2.1.18) | protein | 379 | 6% helix, 47% strand | P29768 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.66 | 0.80 | 30 | GOL |
| 2 | 188 | 0.54 | 0.79 | 31 | K, PO4, GOL |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P29768
- Elsewhere: RCSB PDB 3SIL · PDBe 3SIL · UniProt P29768
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