Research workbench
Structure of GH32 hydrolase from bifidobacterium adolescentis in complex with frutose
Analyse Structure of GH32 hydrolase from bifidobacterium adolescentis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NUN
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-fructofuranosidase
- UniProt
- A0A1X2ZCY9
- Ligands
- FRU
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-fructofuranosidase | protein | 516 | 8% helix, 50% strand | A0A1X2ZCY9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.58 | 0.79 | 24 | EDO, FRU |
| 2 | 178 | 0.54 | 0.79 | 24 | empty |
| 3 | 100 | 0.44 | 0.79 | 24 | EDO |
Compared structures
- 6NUN · Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose · 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 A0A1X2ZCY9
- Elsewhere: RCSB PDB 6NUN · PDBe 6NUN · UniProt A0A1X2ZCY9
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