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N2 neuraminidase of A/TANZANIA/205/2010 H3N2 in complex with sialic acid

Analyse N2 neuraminidase of A/TANZANIA/205/2010 H3N2 in complex with sialic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GZQ
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nueraminidase
Ligands: NAG, MAN, BMA, SIA, CA
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nueraminidase	protein	388	2% helix, 47% strand	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies
BMA · beta-D-mannopyranose · sugar
SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A
CA · Calcium ion · metal · 2 copies · 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	175	0.56	0.81	23	SIA
2	62	0.37	0.79	25	empty

Modifications

Observed in the structure: 9 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

4GZQ · N2 neuraminidase of A/Tanzania/205/2010 H3N2 in complex with sialic acid · 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
Elsewhere: RCSB PDB 4GZQ · PDBe 4GZQ

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