Research workbench
Glycoside hydrolase BT3686 bound to glucuronic acid
Analyse Glycoside hydrolase BT3686 bound to glucuronic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MUL
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neuraminidase
- UniProt
- Q8A1H5
- Ligands
- BDP
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neuraminidase | protein | 378 | 4% helix, 47% strand | Q8A1H5 |
Ligands and binding sites
- BDP · beta-D-glucopyranuronic acid · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 820 | 0.78 | 0.82 | 56 | empty |
| 2 | 133 | 0.45 | 0.77 | 25 | BDP |
| 3 | 61 | 0.36 | 0.78 | 21 | empty |
| 4 | 59 | 0.31 | 0.76 | 17 | empty |
Compared structures
- 5MUL · Glycoside Hydrolase BT3686 bound to Glucuronic Acid · 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 Q8A1H5
- Elsewhere: RCSB PDB 5MUL · PDBe 5MUL · UniProt Q8A1H5
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