Research workbench
Structure of E. COLI beta-glucuronidase complex with uronic isofagomine
Analyse Structure of E. COLI beta-glucuronidase complex with uronic isofagomine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LEG
- Type
- protein
- Length
- 2,397 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- W8SYR0
- Ligands
- SJ5
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 602 | — | W8SYR0 |
| C | — | protein | 599 | — | W8SYR0 |
| D | — | protein | 594 | — | W8SYR0 |
Ligands and binding sites
- SJ5 · (3S,4R,5R)-4,5-dihydroxypiperidine-3-carboxylic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LEG · Structure of E. coli beta-glucuronidase complex with uronic isofagomine · the same entry in another collection · chain B against B, 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 6LEG · PDBe 6LEG · UniProt W8SYR0
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