Research workbench

Anhui N9-laninamivir

Analyse Anhui N9-laninamivir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MWU
Type: protein
Length: 388 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuraminidase
UniProt: A0A024E3Q2
Ligands: LNV, MAN, NAG, BMA, CA
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuraminidase	protein	388	4% helix, 46% strand	A0A024E3Q2

Ligands and binding sites

LNV · 5-acetamido-2,6-anhydro-4-carbamimidamido-3,4,5-trideoxy-7-O-methyl-D-glycero-D-galacto-non-2-enonic acid · ligand · chains A
MAN · alpha-D-mannopyranose · sugar · 6 copies
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
BMA · beta-D-mannopyranose · sugar
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	258	0.61	0.80	40	LNV

Modifications

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

Compared structures

4MWU · Anhui N9-laninamivir · 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 A0A024E3Q2
Elsewhere: RCSB PDB 4MWU · PDBe 4MWU · UniProt A0A024E3Q2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.