Research workbench
Structure of beta-glycosidase from sulfolobus solfataricus in complex with 2-deoxy-2-fluoro-galactose
Analyse Structure of beta-glycosidase from sulfolobus solfataricus in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UWR
- Type
- protein
- Length
- 973 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- P22498
- Ligands
- GAF
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactosidase (EC 3.2.1.23) | protein | 489 | 41% helix, 18% strand | P22498 |
| B | Beta-galactosidase (EC 3.2.1.23) | protein | 484 | 40% helix, 18% strand | P22498 |
Ligands and binding sites
- GAF · 2-deoxy-2-fluoro-alpha-D-galactopyranose · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains B
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 | 734 | 0.71 | 0.78 | 68 | GAF |
| 2 | 636 | 0.71 | 0.79 | 54 | GAF |
| 3 | 80 | 0.30 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 124 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 1UWR · Structure of beta-glycosidase from Sulfolobus solfataricus in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P22498 · AlphaFold monomer V2.0 prediction for beta-galactosidase (P22498) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P22498
- Elsewhere: RCSB PDB 1UWR · PDBe 1UWR · UniProt P22498
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