MolNFT v1 · #86470 · protein

H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis

4B7N: “H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and…”. X-ray diffraction, 3 ligands (ZMR, NAG, CA), 1 pocket (best druggability 0.63). MolNFT v1 #86470 on GenesisL1: 3D…

PDB: 4B7N
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neuraminidase
UniProt: F8UU09
Ligands: ZMR, NAG, CA
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Neuraminidase	protein	386	3% helix, 45% strand	F8UU09

Ligands and binding sites

ZMR · Zanamivir · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 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

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	266	0.63	0.81	41	ZMR

Modifications

Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

4B7N · H1N1 2009 Pandemic Influenza Virus: Resistance of the I223R Neuraminidase Mutant… · 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 F8UU09
Elsewhere: RCSB PDB 4B7N · PDBe 4B7N · UniProt F8UU09

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