Research workbench
Structure of E. COLI beta-glucuronidase complex with C6-hexyl uronic isofagomine
Analyse Structure of E. COLI beta-glucuronidase complex with C6-hexyl uronic isofagomine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LEL
- Type
- protein
- Length
- 1,184 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- W8SYR0
- Ligands
- E8X
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 597 | — | W8SYR0 |
| B | — | protein | 587 | — | W8SYR0 |
Ligands and binding sites
- E8X · (2~{S},3~{S},4~{R},5~{R})-2-hexyl-4,5-bis(oxidanyl) piperidine-3-carboxylic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LEL · Structure of E. coli beta-glucuronidase complex with C6-hexyl uronic isofagomine · 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 W8SYR0
- Elsewhere: RCSB PDB 6LEL · PDBe 6LEL · UniProt W8SYR0
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