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Maltose-induced structure of the human cytolsolic sialidase NEU2

Analyse Maltose-induced structure of the human cytolsolic sialidase NEU2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SO7
Type: protein
Length: 361 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sialidase 2
EC: 3.2.1.18
UniProt: Q9Y3R4
Ligands: CL
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sialidase 2 (EC 3.2.1.18)	protein	361	8% helix, 52% strand	Q9Y3R4

Ligands and binding sites

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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	327	0.64	0.80	30	empty
2	118	0.38	0.74	25	empty

Compared structures

1SO7 · Maltose-induced structure of the human cytolsolic sialidase Neu2 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y3R4 · AlphaFold monomer V2.0 prediction for sialidase-2 (Q9Y3R4) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9Y3R4
Elsewhere: RCSB PDB 1SO7 · PDBe 1SO7 · UniProt Q9Y3R4

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