Research workbench
Complex structure of beta-galactosidase from trichoderma reesei with galactose
Analyse Complex structure of beta-galactosidase from trichoderma reesei with galactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OGR
- Type
- protein
- Length
- 986 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- Q70SY0
- Ligands
- MAN, NAG, BMA, GLC, GAL
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactosidase (EC 3.2.1.23) | protein | 986 | 15% helix, 32% strand | Q70SY0 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 10 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.71 | 0.99 | 22 | empty |
| 2 | 151 | 0.56 | 0.82 | 20 | empty |
| 3 | 141 | 0.54 | 0.81 | 30 | empty |
| 4 | 68 | 0.47 | 0.83 | 17 | empty |
| 5 | 101 | 0.42 | 0.77 | 23 | GAL |
Modifications
Observed in the structure: 5 glycan, 1 disulfide (N-glycosylation, disulfide).
Compared structures
- 3OGR · Complex structure of beta-galactosidase from Trichoderma reesei with galactose · 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 Q70SY0
- Elsewhere: RCSB PDB 3OGR · PDBe 3OGR · UniProt Q70SY0
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