Research workbench
Monomer structure of hyperthermophilic beta-glucosidase mutant forming a dodecameric structure in the crystal form
Analyse Monomer structure of hyperthermophilic beta-glucosidase mutant forming a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WQ8
- Type
- protein
- Length
- 5,344 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucosidase
- EC
- 3.2.1.21
- UniProt
- Q51723
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, H, L | Beta-glucosidase (EC 3.2.1.21) | protein | 448 | 44% helix, 18% strand | Q51723 |
| B, C, D, E, F, I, J, K | Beta-glucosidase (EC 3.2.1.21) | protein | 444 | 45% helix, 17% strand | Q51723 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 893 | 0.74 | 0.78 | 79 | empty |
| 2 | 848 | 0.73 | 0.78 | 69 | empty |
| 3 | 818 | 0.72 | 0.77 | 89 | empty |
| 4 | 571 | 0.72 | 0.80 | 50 | empty |
| 5 | 600 | 0.72 | 0.79 | 47 | empty |
Interfaces
24 interfaces between chains.
- C–D · 678 Ų buried · 2 hydrogen bonds · protein-protein
- G–H · 669 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 651 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 646 Ų buried · 3 hydrogen bonds · protein-protein
- K–L · 611 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3WQ8 · Monomer structure of hyperthermophilic beta-glucosidase mutant forming a dodecameric… · the same entry in another collection · chain I against I, 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 Q51723
- Elsewhere: RCSB PDB 3WQ8 · PDBe 3WQ8 · UniProt Q51723
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