Research workbench
Crystal structure of perdeuterated pll lectin in complex with L-fucose
Analyse Crystal structure of perdeuterated pll lectin in complex with L-fucose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BB4
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A329WTS5
- Ligands
- FUL, FUC
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 354 | — | A0A329WTS5 |
Ligands and binding sites
- FUL · beta-L-fucopyranose · sugar · 4 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · 3 copies · chains A
- GOL · Glycerol · additive · 9 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BB4 · Crystal structure of perdeuterated PLL lectin in complex with L-fucose · 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 A0A329WTS5
- Elsewhere: RCSB PDB 7BB4 · PDBe 7BB4 · UniProt A0A329WTS5
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