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Influenza neuraminidase in complex with a novel antiviral compound

Analyse Influenza neuraminidase in complex with a novel antiviral compound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MJU
Type: protein
Length: 389 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuraminidase
EC: 3.2.1.18
UniProt: Q07599
Ligands: 27S, CA
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuraminidase (EC 3.2.1.18)	protein	389	5% helix, 46% strand	Q07599

Ligands and binding sites

27S · (5R,9R,10S)-10-(acetylamino)-2-amino-4-oxo-9-(pentan-3-yloxy)-1-thia-3-azaspiro[4.5]deca-2,6-diene-7-carboxylic acid · ligand · chains A
CA · Calcium ion · metal · 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	427	0.65	0.79	52	27S
2	64	0.32	0.75	14	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

4MJU · Influenza Neuraminidase in complex with a novel antiviral compound · the same entry in another collection · 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 Q07599
Elsewhere: RCSB PDB 4MJU · PDBe 4MJU · UniProt Q07599

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