Research workbench
Bacterial chitobiase, glycosyl hydrolase family 20
Analyse Bacterial chitobiase, glycosyl hydrolase family 20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QBA
- Type
- protein
- Length
- 858 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Serratia marcescens
- Molecule
- Chitobiase
- EC
- 3.2.1.52
- UniProt
- Q54468
- Ligands
- SO4
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitobiase (EC 3.2.1.52) | protein | 858 | 30% helix, 22% strand | Q54468 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 761 | 0.76 | 0.80 | 65 | empty |
| 2 | 382 | 0.67 | 0.80 | 39 | empty |
| 3 | 243 | 0.51 | 0.75 | 24 | empty |
| 4 | 135 | 0.49 | 0.79 | 17 | empty |
| 5 | 138 | 0.43 | 0.76 | 24 | SO4 |
Modifications
Observed in the structure: 3 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 Q54468
- Elsewhere: RCSB PDB 1QBA · PDBe 1QBA · UniProt Q54468
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