Research workbench
Structure of fructofuranosidase from xanthophyllomyces dendrorhous
Analyse Structure of fructofuranosidase from xanthophyllomyces dendrorhous in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ANN
- Type
- protein
- Length
- 1,248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-fructofuranosidase
- EC
- 3.2.1.26
- UniProt
- J7HDY4
- Ligands
- NAG, MAN, BMA
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-fructofuranosidase (EC 3.2.1.26) | protein | 624 | 7% helix, 43% strand | J7HDY4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 38 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 20 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, B
- GOL · Glycerol · additive · 4 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 869 | 0.75 | 0.79 | 121 | empty |
| 2 | 198 | 0.73 | 0.90 | 46 | empty |
| 3 | 434 | 0.65 | 0.78 | 39 | GOL |
| 4 | 412 | 0.64 | 0.78 | 37 | GOL |
| 5 | 426 | 0.60 | 0.76 | 50 | NAG, GOL |
Interfaces
1 interface between chains.
- A–B · 392 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 glycan, 2 disulfide (N-glycosylation, disulfide, glycosylation).
Compared structures
- 5ANN · Structure of fructofuranosidase from Xanthophyllomyces dendrorhous · 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 J7HDY4
- Elsewhere: RCSB PDB 5ANN · PDBe 5ANN · UniProt J7HDY4
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