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Sugar binding protein - human galectin-2

Analyse Sugar binding protein - human galectin-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EWS
Type: protein
Length: 2,096 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Galectin-2
UniProt: P05162
Ligands: BGC, GAL
Pockets: 12 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Galectin-2	protein	131	0% helix, 61% strand	P05162

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 8 copies · chains B, C, F, A, D, E, G, O, H, I, J, K, M, N
GAL · beta-D-galactopyranose · sugar · 8 copies · chains B, C, A, D, G, O, H, E, I, F, J, K, M, N

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1197	0.79	0.81	130	BGC, GAL
2	978	0.79	0.81	118	BGC, GAL
3	1199	0.79	0.81	113	BGC, GAL
4	622	0.75	0.82	68	GAL
5	884	0.75	0.79	89	GAL

Interfaces

33 interfaces between chains.

I–O · 813 Å² buried · 17 hydrogen bonds · protein-protein
J–P · 777 Å² buried · 13 hydrogen bonds · protein-protein
E–H · 769 Å² buried · 14 hydrogen bonds · protein-protein
C–K · 766 Å² buried · 13 hydrogen bonds · protein-protein
F–G · 760 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

5EWS · Sugar binding protein - human galectin-2 · the same entry in another collection · chain P against P, TM-score 1.00

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 P05162
Elsewhere: RCSB PDB 5EWS · PDBe 5EWS · UniProt P05162

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