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Crystal structure of full-length E. COLI beta-glucuronidase
Analyse Crystal structure of full-length E. COLI beta-glucuronidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K46
- Type
- protein
- Length
- 1,193 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucuronidase
- EC
- 3.2.1.31
- UniProt
- P05804
- Pockets
- 16 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucuronidase (EC 3.2.1.31) | protein | 597 | 19% helix, 29% strand | P05804 |
| B | Beta-glucuronidase (EC 3.2.1.31) | protein | 596 | 20% helix, 28% strand | P05804 |
Pockets
16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1129 | 0.86 | 0.87 | 111 | empty |
| 2 | 88 | 0.73 | 0.96 | 18 | empty |
| 3 | 66 | 0.72 | 0.97 | 18 | empty |
| 4 | 53 | 0.70 | 0.98 | 18 | empty |
| 5 | 57 | 0.70 | 0.97 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1720 Ų buried · 11 hydrogen bonds · protein-protein
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 P05804
- Elsewhere: RCSB PDB 3K46 · PDBe 3K46 · UniProt P05804
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