Research workbench
Human beta-glucuronidase at 2.6 a resolution
Analyse Human beta-glucuronidase at 2.6 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BHG
- Type
- protein
- Length
- 1,222 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucuronidase
- EC
- 3.2.1.31
- UniProt
- P08236
- Ligands
- MAN, NAG, BMA
- Pockets
- 20 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-glucuronidase (EC 3.2.1.31) | protein | 611 | 21% helix, 27% strand | P08236 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 12 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.76 | 0.98 | 22 | empty |
| 2 | 470 | 0.74 | 0.83 | 55 | empty |
| 3 | 249 | 0.71 | 0.86 | 43 | empty |
| 4 | 58 | 0.70 | 0.97 | 20 | empty |
| 5 | 175 | 0.63 | 0.85 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 650 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 glycan (N-glycosylation).
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 P08236
- Elsewhere: RCSB PDB 1BHG · PDBe 1BHG · UniProt P08236
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