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The crystal structure of the glycoside hydrolase bglx from P. aeruginosa
Analyse The crystal structure of the glycoside hydrolase bglx from P. aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R5I
- Type
- protein
- Length
- 1,460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic beta-glucosidase
- UniProt
- Q9I311
- Ligands
- MG, SO4
- Pockets
- 16 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic beta-glucosidase | protein | 733 | 34% helix, 20% strand | Q9I311 |
| B | Periplasmic beta-glucosidase | protein | 727 | 34% helix, 19% strand | Q9I311 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.86 | 0.96 | 36 | empty |
| 2 | 88 | 0.75 | 0.97 | 22 | empty |
| 3 | 96 | 0.74 | 0.96 | 22 | empty |
| 4 | 446 | 0.70 | 0.81 | 49 | empty |
| 5 | 438 | 0.64 | 0.77 | 60 | empty |
Interfaces
1 interface between chains.
- A–B · 3292 Ų buried · 73 hydrogen bonds · protein-protein
Compared structures
- 6R5I · The crystal structure of the Glycoside Hydrolase BglX from P. aeruginosa · 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 Q9I311
- Elsewhere: RCSB PDB 6R5I · PDBe 6R5I · UniProt Q9I311
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