Research workbench
Structure of the 6-phospho-beta glucosidase from thermotoga maritima at 2.85 ångström resolution in the monoclinic form
Analyse Structure of the 6-phospho-beta glucosidase from thermotoga maritima at 2.85… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UP4
- Type
- protein
- Length
- 3,228 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 6-phospho-beta-glucosidase
- EC
- 3.2.1.6
- UniProt
- Q9X108
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 8 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 410 | 50% helix, 17% strand | Q9X108 |
| B | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 403 | 49% helix, 17% strand | Q9X108 |
| C | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 408 | 50% helix, 17% strand | Q9X108 |
| D | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 400 | 50% helix, 18% strand | Q9X108 |
| E | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 396 | 51% helix, 17% strand | Q9X108 |
| F | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 399 | 50% helix, 18% strand | Q9X108 |
| G | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 409 | 50% helix, 17% strand | Q9X108 |
| H | 6-phospho-beta-glucosidase (EC 3.2.1.6) | protein | 403 | 50% helix, 17% strand | Q9X108 |
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 | 872 | 0.80 | 0.82 | 68 | empty |
| 2 | 396 | 0.80 | 0.88 | 58 | empty |
| 3 | 845 | 0.79 | 0.82 | 86 | empty |
| 4 | 811 | 0.79 | 0.82 | 82 | empty |
| 5 | 814 | 0.78 | 0.82 | 84 | empty |
Interfaces
10 interfaces between chains.
- A–B · 1708 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1704 Ų buried · 18 hydrogen bonds · protein-protein
- G–H · 1690 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1689 Ų buried · 20 hydrogen bonds · protein-protein
- E–H · 951 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 56 modified (engineered).
Compared structures
- 1UP4 · Structure of the 6-phospho-beta glucosidase from Thermotoga maritima at 2.85 Angstrom… · the same entry in another collection · chain H against H, TM-score 1.00
- Q9X108 · AlphaFold monomer V2.0 prediction for 6-phospho-beta-glucosidase bglt (Q9X108) · a predicted model of the same protein · chain F against A, TM-score 0.99
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 Q9X108
- Elsewhere: RCSB PDB 1UP4 · PDBe 1UP4 · UniProt Q9X108
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