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Sialidase complexed with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid

Analyse Sialidase complexed with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EUS
Type: protein
Length: 358 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sialidase
EC: 3.2.1.18
UniProt: Q02834
Ligands: DAN
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sialidase (EC 3.2.1.18)	protein	358	3% helix, 44% strand	Q02834

Ligands and binding sites

DAN · 2-deoxy-2,3-dehydro-N-acetyl-neuraminic acid · ligand · 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	214	0.70	0.87	38	empty
2	104	0.44	0.78	19	DAN

Compared structures

1EUS · Sialidase complexed with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid · the same entry in another collection · chain A against A, TM-score 1.00
Q02834 · AlphaFold monomer V2.0 prediction for sialidase (Q02834) · a predicted model of the same protein · chain A against A, 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 Q02834
Elsewhere: RCSB PDB 1EUS · PDBe 1EUS · UniProt Q02834

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