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Influenza neuraminidase in complex with a stereomutated analogue of oseltamivir carboxylate

Analyse Influenza neuraminidase in complex with a stereomutated analogue of oseltamivir… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M3M
Type: protein
Length: 390 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuraminidase
UniProt: Q0A480
Ligands: 22N, NAG, 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	protein	390	5% helix, 46% strand	Q0A480

Ligands and binding sites

22N · (3R,4S,5S)-4-(acetylamino)-5-amino-3-(pentan-3-yloxy)cyclohex-1-ene-1-carboxylic acid · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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	364	0.65	0.80	41	22N
2	75	0.32	0.74	17	empty

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

4M3M · Influenza Neuraminidase in complex with a stereomutated analogue of Oseltamivir… · 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 Q0A480
Elsewhere: RCSB PDB 4M3M · PDBe 4M3M · UniProt Q0A480

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