GL1X · GenesisL1 explorer

Research workbench

X-ray crystal structure of human galectin-1

Analyse X-ray crystal structure of human galectin-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GZW
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
BGC, GAL, SO4
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 60% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGalectin-1protein1340% helix, 60% strandP09382

Ligands and binding sites

  • BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · chains A
  • BME · Beta-mercaptoethanol · additive · 5 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.490.8021empty
2620.400.8020empty

Interfaces

1 interface between chains.

  • A–B · 609 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 covalent, 1 modified (additive adduct, oxidation).

Compared structures

  • 1GZW · X-ray crystal structure of human galectin-1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P09382 · AlphaFold monomer V2.0 prediction for galectin-1 (P09382) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.