Research workbench
Bifunctional XYLOSIDASE/GLUCOSIDASE lxyl with intermediate substrate xylose for 2 min
Analyse Bifunctional XYLOSIDASE/GLUCOSIDASE lxyl with intermediate substrate xylose for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F95
- Type
- protein
- Length
- 3,024 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G8GLP2
- Ligands
- BKR, XYL, XYZ, NAG, MAN, BMA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 756 | — | G8GLP2 |
Ligands and binding sites
- BKR · Deacetyltaxol · ligand · 2 copies · chains A, B
- XYL · Xylitol · ligand · chains A
- XYZ · beta-D-xylofuranose · ligand · chains B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 39 copies · chains A, B, C, D
- MAN · alpha-D-mannopyranose · sugar · 24 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 9 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 G8GLP2
- Elsewhere: RCSB PDB 7F95 · PDBe 7F95 · UniProt G8GLP2
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