MolNFT v1 · #21800 · protein
Structure of S-lectin, a developmentally regulated vertebrate beta- galactoside binding protein
1SLT · Bovine galectin-1: “Structure of S-lectin, a developmentally regulated vertebrate beta- galactoside binding protein”. X-ray diffraction, 3 ligands (NDG, GAL, CL), 2 pockets (best druggability 0.36). MolNFT v1 #21800 on GenesisL1: 3D…
- PDB
- 1SLT
- Type
- protein
- Length
- 265 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bovine galectin-1
- UniProt
- P11116
- Ligands
- NDG, GAL, CL
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bovine galectin-1 | protein | 133 | 0% helix, 62% strand | P11116 |
| B | Bovine galectin-1 | protein | 132 | 0% helix, 65% strand | P11116 |
Ligands and binding sites
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
- CL · Chloride ion · ion · chains 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 | 70 | 0.36 | 0.77 | 13 | empty |
| 2 | 64 | 0.34 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 564 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (oxidation).
Compared structures
- 1SLT · Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside binding… · 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 0.99
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 1SLT · PDBe 1SLT · UniProt P11116
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