Research workbench
Crystal structure of the double mutant L167W / P172L of the beta- glucosidase from trichoderma harzianum
Analyse Crystal structure of the double mutant L167W / P172L of the beta- glucosidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EFU
- Type
- protein
- Length
- 929 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucosidase
- EC
- 3.2.1.21
- UniProt
- A0A127SA86
- Ligands
- NO3
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-glucosidase (EC 3.2.1.21) | protein | 465 | 43% helix, 16% strand | A0A127SA86 |
| B | Beta-glucosidase (EC 3.2.1.21) | protein | 464 | 45% helix, 16% strand | A0A127SA86 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.70 | 0.82 | 35 | empty |
| 2 | 614 | 0.67 | 0.76 | 50 | empty |
| 3 | 302 | 0.66 | 0.81 | 36 | NO3 |
| 4 | 311 | 0.65 | 0.81 | 37 | NO3 |
| 5 | 69 | 0.42 | 0.81 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1028 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6EFU · Crystal structure of the double mutant L167W / P172L of the beta-glucosidase from… · 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 A0A127SA86
- Elsewhere: RCSB PDB 6EFU · PDBe 6EFU · UniProt A0A127SA86
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