Research workbench
Bacterial chitobiase complexed with chitobiose (dinag)
Analyse Bacterial chitobiase complexed with chitobiose (dinag) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QBB
- Type
- protein
- Length
- 858 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitobiase
- EC
- 3.2.1.52
- UniProt
- Q54468
- Ligands
- NAG, SO4
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitobiase (EC 3.2.1.52) | protein | 858 | 29% helix, 22% strand | Q54468 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- 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 | 839 | 0.78 | 0.81 | 71 | NAG |
| 2 | 355 | 0.66 | 0.80 | 45 | empty |
| 3 | 235 | 0.52 | 0.76 | 24 | empty |
| 4 | 117 | 0.49 | 0.80 | 17 | empty |
| 5 | 139 | 0.43 | 0.76 | 25 | 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 1QBB · PDBe 1QBB · UniProt Q54468
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