Research workbench
Trypanosoma rangeli sialidase
Analyse Trypanosoma rangeli sialidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N1S
- Type
- protein
- Length
- 628 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sialidase
- EC
- 3.2.1.18
- UniProt
- O44049
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sialidase (EC 3.2.1.18) | protein | 628 | 7% helix, 47% strand | O44049 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 257 | 0.59 | 0.79 | 32 | SO4 |
| 2 | 253 | 0.58 | 0.79 | 26 | empty |
| 3 | 164 | 0.47 | 0.77 | 29 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1N1S · Trypanosoma rangeli sialidase · the same entry in another collection · chain A against A, TM-score 1.00
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 O44049
- Elsewhere: RCSB PDB 1N1S · PDBe 1N1S · UniProt O44049
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