Research workbench
Crystal structure of beta-D-glucoside glucohydrolase from trichoderma reesei
Analyse Crystal structure of beta-D-glucoside glucohydrolase from trichoderma reesei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I8D
- Type
- protein
- Length
- 1,425 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-D-glucoside glucohydrolase
- EC
- 3.2.1.21
- UniProt
- Q12715
- Ligands
- MAN, NAG, BMA, BGC
- Pockets
- 14 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-D-glucoside glucohydrolase (EC 3.2.1.21) | protein | 711 | 29% helix, 22% strand | Q12715 |
| B | Beta-D-glucoside glucohydrolase (EC 3.2.1.21) | protein | 714 | 29% helix, 23% strand | Q12715 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 11 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains A, B
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.80 | 0.96 | 27 | empty |
| 2 | 425 | 0.73 | 0.84 | 60 | empty |
| 3 | 329 | 0.62 | 0.79 | 45 | empty |
| 4 | 84 | 0.56 | 0.86 | 21 | empty |
| 5 | 161 | 0.53 | 0.80 | 27 | BGC |
Interfaces
1 interface between chains.
- A–B · 1022 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 4I8D · Crystal Structure of Beta-D-glucoside glucohydrolase from Trichoderma reesei · 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 Q12715
- Elsewhere: RCSB PDB 4I8D · PDBe 4I8D · UniProt Q12715
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.