Research workbench
Complex of human galectin-1 and GALBETA1-4GLCNAC
Analyse Complex of human galectin-1 and GALBETA1-4GLCNAC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y1U
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galectin-1
- UniProt
- P09382
- Ligands
- MAG, GAL
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Galectin-1 | protein | 133 | 0% helix, 64% strand | P09382 |
Ligands and binding sites
- MAG · methyl 2-acetamido-2-deoxy-beta-D-glucopyranoside · sugar · 2 copies · chains B, A
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains B, A
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 | 132 | 0.45 | 0.77 | 18 | empty |
| 2 | 103 | 0.43 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- B–A · 571 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (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 4Y1U · PDBe 4Y1U · UniProt P09382
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