Research workbench
Crystal structure of human galectin-1 in complex with lactobionic acid
Analyse Crystal structure of human galectin-1 in complex with lactobionic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OY8
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galectin-1
- UniProt
- P09382
- Ligands
- GCO, GAL
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Galectin-1 | protein | 134 | 2% helix, 63% strand | P09382 |
Ligands and binding sites
- GCO · D-gluconic acid · ligand · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.45 | 0.80 | 17 | empty |
| 2 | 71 | 0.39 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 623 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (artifact, oxidation).
Compared structures
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 P09382
- Elsewhere: RCSB PDB 3OY8 · PDBe 3OY8 · UniProt P09382
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