Research workbench
Crystal structure of the beta-glucosidase BGL15
Analyse Crystal structure of the beta-glucosidase BGL15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JFP
- Type
- protein
- Length
- 888 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-glucosidase 15
- Ligands
- BGC
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Beta-glucosidase 15 | protein | 444 | 44% helix, 17% strand | — |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 511 | 0.71 | 0.80 | 54 | empty |
| 2 | 506 | 0.70 | 0.80 | 53 | BGC |
| 3 | 158 | 0.45 | 0.76 | 24 | empty |
| 4 | 161 | 0.42 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- B–A · 1033 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6JFP · Crystal structure of the beta-glucosidase Bgl15 · the same entry in another collection · chain B against B, 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
- Elsewhere: RCSB PDB 6JFP · PDBe 6JFP
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