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Crystal structure of mouse galectin-9 N-terminal crd in complex with N-acetyllactosamine dimer

Analyse Crystal structure of mouse galectin-9 N-terminal crd in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D6O
Type: protein
Length: 151 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lectin, galactose binding, soluble 9
UniProt: Q5SXE6
Ligands: NAG, GAL
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Lectin, galactose binding, soluble 9	protein	151	2% helix, 56% strand	Q5SXE6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains X
GAL · beta-D-galactopyranose · sugar · 2 copies · chains X
GOL · Glycerol · additive · chains X

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.30	0.74	16	empty

Compared structures

2D6O · Crystal structure of mouse galectin-9 N-terminal CRD in complex with N-acetyllactosamine… · the same entry in another collection · chain X against X, 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 Q5SXE6
Elsewhere: RCSB PDB 2D6O · PDBe 2D6O · UniProt Q5SXE6

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