Research workbench
Glycoside hydrolase BT_0996
Analyse Glycoside hydrolase BT_0996 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MUI
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8A921
- Ligands
- 8OQ, FUB, 8PK, RAM, GAL, ARA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 352 | — | Q8A921 |
Ligands and binding sites
- 8OQ · alpha-D-aceric acid · ligand · chains A
- FUB · beta-L-arabinofuranose · ligand · chains A
- 8PK · 4-O-[(1R)-1-hydroxyethyl]-2-O-methyl-alpha-L-fucopyranose · ligand · chains A
- RAM · alpha-L-rhamnopyranose · sugar · 3 copies · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- ARA · alpha-L-arabinopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MUI · Glycoside hydrolase BT_0996 · 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 Q8A921
- Elsewhere: RCSB PDB 5MUI · PDBe 5MUI · UniProt Q8A921
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