Research workbench
Leech intramolecular trans-sialidase complexed with 2,7- anhydro-NEU5AC prepared by soaking with 3'-sialyllactose
Analyse Leech intramolecular trans-sialidase complexed with 2,7- anhydro-NEU5AC… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SLI
- Type
- protein
- Length
- 679 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intramolecular trans-sialidase
- EC
- 3.2.1.18
- UniProt
- Q27701
- Ligands
- SKD
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Intramolecular trans-sialidase (EC 3.2.1.18) | protein | 679 | 5% helix, 46% strand | Q27701 |
Ligands and binding sites
- SKD · 2-acetylamino-7-(1,2-dihydroxy-ethyl)-3-hydroxy-6,8-dioxa-bicyclo[3.2.1]octane-5-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 307 | 0.69 | 0.84 | 40 | empty |
| 2 | 275 | 0.60 | 0.79 | 38 | empty |
| 3 | 223 | 0.59 | 0.81 | 30 | SKD |
| 4 | 183 | 0.46 | 0.75 | 23 | empty |
| 5 | 53 | 0.24 | 0.73 | 16 | empty |
Compared structures
- 3SLI · Leech intramolecular trans-sialidase complexed with 2,7-anhydro-NEU5AC prepared by… · the same entry in another collection · chain A against A, TM-score 1.00
- Q27701 · AlphaFold monomer V2.0 prediction for anhydrosialidase (Q27701) · a predicted model of the same protein · 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 Q27701
- Elsewhere: RCSB PDB 3SLI · PDBe 3SLI · UniProt Q27701
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