Research workbench
Crystal structure of BHGH81 mutant in complex with laminaro-tetraose
Analyse Crystal structure of BHGH81 mutant in complex with laminaro-tetraose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UPN
- Type
- protein
- Length
- 752 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9KG76
- Ligands
- BGC, GLC, PO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 752 | — | Q9KG76 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 10 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- PO4 · Phosphate ion · ion · 9 copies · chains A
- EDO · 1,2-ethanediol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5UPN · Crystal structure of BhGH81 mutant in complex with laminaro-tetraose · 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 Q9KG76
- Elsewhere: RCSB PDB 5UPN · PDBe 5UPN · UniProt Q9KG76
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