Research workbench
X-ray crystal structure of Xenopus laevis galectin-Ib
Analyse X-ray crystal structure of Xenopus laevis galectin-Ib in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WUD
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.68
- Source
- Xenopus laevis
- Molecule
- Galectin
- UniProt
- Q98UD4
- Ligands
- GLC, GAL, SO4
Structure
x-ray diffraction · resolution 1.68 · 1 distinct chain · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galectin | protein | 132 | 0% helix, 63% strand | Q98UD4 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3WUD · X-ray crystal structure of xenopus laevis galectin-ib · 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 Q98UD4
- Elsewhere: RCSB PDB 3WUD · PDBe 3WUD · UniProt Q98UD4
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