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Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants

Analyse Refined atomic structures of N9 subtype influenza virus neuraminidase and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NN9
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuraminidase N9
EC: 3.2.1.18
UniProt: P03472
Ligands: MAN, NAG, CA
Pockets: 2 · best druggability 0.61

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuraminidase N9 (EC 3.2.1.18)	protein	388	3% helix, 44% strand	P03472

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · 5 copies
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · 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	267	0.61	0.80	44	empty
2	53	0.34	0.79	14	empty

Modifications

Observed in the structure: 9 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

5NN9 · Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P03472
Elsewhere: RCSB PDB 5NN9 · PDBe 5NN9 · UniProt P03472

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