MolNFT v1 · #21783 · protein
X-ray crystallography reveals crosslinking of mammalian lectin (galectin-1) by biantennary complex type saccharides
1SLA · Bovine galectin-1: “X-ray crystallography reveals crosslinking of mammalian lectin (galectin-1) by biantennary complex type…”. X-ray diffraction, 4 ligands (NAG, MAN, GAL), 2 pockets (best druggability 0.45). MolNFT v1 #21783 on…
- PDB
- 1SLA
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bovine galectin-1
- UniProt
- P11116
- Ligands
- NAG, MAN, GAL, BMA
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bovine galectin-1 | protein | 134 | 0% helix, 65% strand | P11116 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
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 | 65 | 0.45 | 0.82 | 16 | empty |
| 2 | 142 | 0.44 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 564 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1SLA · X-ray crystallography reveals crosslinking of mammalian lectin (galectin-1) by… · the same entry in another collection · chain A against A, TM-score 1.00
- P11116 · AlphaFold monomer V2.0 prediction for galectin-1 (P11116) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P11116
- Elsewhere: RCSB PDB 1SLA · PDBe 1SLA · UniProt P11116
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