Research workbench
Crystal structure of 1,2-a-L-fucosidase from bifidobacterium bifidum in complexes with products
Analyse Crystal structure of 1,2-a-L-fucosidase from bifidobacterium bifidum in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EAE
- Type
- protein
- Length
- 887 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-fucosidase
- EC
- 3.2.1.63
- UniProt
- Q6JV24
- Ligands
- GLC, GAL, FUC, FUL, CA
- Pockets
- 8 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-fucosidase (EC 3.2.1.63) | protein | 887 | 31% helix, 25% strand | Q6JV24 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- FUL · beta-L-fucopyranose · sugar · chains A
- CA · Calcium ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.56 | 0.81 | 28 | empty |
| 2 | 70 | 0.46 | 0.82 | 15 | GAL, FUC, FUL |
| 3 | 156 | 0.45 | 0.75 | 25 | empty |
| 4 | 116 | 0.42 | 0.77 | 22 | empty |
| 5 | 87 | 0.42 | 0.79 | 23 | empty |
Compared structures
- 2EAE · Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complexes with… · 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 Q6JV24
- Elsewhere: RCSB PDB 2EAE · PDBe 2EAE · UniProt Q6JV24
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.