Research workbench
Crystal structure of beta-glucuronidase from acidobacterium capsulatum at 1.24 ångström resolution
Analyse Crystal structure of beta-glucuronidase from acidobacterium capsulatum at 1.24… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PSH
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucuronidase
- UniProt
- C1F2K5
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucuronidase | protein | 448 | 30% helix, 31% strand | C1F2K5 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.55 | 0.77 | 32 | empty |
| 2 | 170 | 0.49 | 0.77 | 43 | empty |
| 3 | 86 | 0.41 | 0.78 | 17 | empty |
| 4 | 58 | 0.33 | 0.77 | 19 | empty |
Compared structures
- 7PSH · Crystal structure of beta-glucuronidase from Acidobacterium capsulatum at 1.24 Angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
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 C1F2K5
- Elsewhere: RCSB PDB 7PSH · PDBe 7PSH · UniProt C1F2K5
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