Research workbench

Crystal structure of a protease-resistant mutant form of human galectin-8

Analyse Crystal structure of a protease-resistant mutant form of human galectin-8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FQZ
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin-8
UniProt: O00214
Ligands: BGC, GAL
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Galectin-8	protein	291	3% helix, 54% strand	O00214

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A
EDO · 1,2-ethanediol · additive · 10 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	181	0.50	0.77	26	empty
2	72	0.37	0.78	16	empty

Compared structures

4FQZ · Crystal structure of a protease-resistant mutant form of human galectin-8 · the same entry in another collection · chain A against A, TM-score 1.00
O00214 · AlphaFold monomer V2.0 prediction for galectin-8 (O00214) · a predicted model of the same protein · chain A against A, TM-score 0.56

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 O00214
Elsewhere: RCSB PDB 4FQZ · PDBe 4FQZ · UniProt O00214

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