1NNC	Hydrolase (O-Glucosyl)	date	Mar 15, 1995
title	Influenza Virus Neuraminidase Subtype N9 (Tern) Complexed With 4-Guanidino-Neu5ac2en Inhibitor
authors	J.N.Varghese, P.M.Colman
compound		source
Molecule: Neuraminidase N9 Chain: A Synonym: Sialidase, Hydrolase (O-Glycosyl) Ec: 3.2.1.18		Organism_scientific: Influenza A Virus (Aternaustraliag70c1975(H11n9)); Organism_taxid: 384509 Strain: Aternaustraliag70c75
symmetry	Space Group: I 4 3 2	R_factor 0.156 R_Free NULL
crystal cell	length a length b length c angle alpha angle beta angle gamma 182.800 182.800 182.800 90.00 90.00 90.00
method	X-Ray Diffraction	resolution	1 Å
ligand	BMA, CA, MAN, NAG, ZMR	enzyme	Exo-alpha-sialidase;. Neuraminidase;. Sialidase;. Alpha-neuraminidase;. Acetylneuraminidase. Hydrolase E.C.3.2.1.18 BRENDA
related structures	by homologous chain: 1F8B, 1L7F
domain	The transmembrane domain also plays a role in lipid raft association (by similarity). Intact n-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain.
similarity	Belongs to the glycosyl hydrolase 34 family.[Neur]
subunit	Homotetramer (by similarity).
catalytic activ.	Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
post-translat. modifications	N-glycosylated (by similarity).
subcellular loc.	Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. Type ii membrane protein. In the virion, forms a mushroom-shaped spike on the surface of the membrane (by similarity).
enzyme regulation	These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Inhibited by the neuraminidase inhibitors zanamivir (relenza) and oseltamivir (tamiflu). Resistance to neuraminidase inhibitors is quite rare.
Gene	NA
function	Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. Otherwise, infection would be limited to one round of replication. Cleaves off the terminal sialic acids on the glycosylated ha during virus budding to facilitate virus release. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. May additionally display a raft-association independent effect on budding.
Gene Ontology	Chain Function Process Component A exo-alpha-sialidase activity... calcium ion binding hydrolase activity hydrolase activity, acting o... metal ion binding carbohydrate metabolic proce... metabolic process plasma membrane membrane integral to membrane virion host cell plasma membrane virion membrane
Primary reference	Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase., Varghese JN, Epa VC, Colman PM, Protein Sci 1995 Jun;4(6):1081-7. PMID:7549872

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (76 Kb) [Save to disk] Biological Unit Coordinates (1nnc.pdb1.gz) 271 Kb CSU: Contacts of Structural Units for 1NNC Likely Quarternary Molecular Structure file(s) for 1NNC Retrieve 1NNC in mmCIF format [Save to disk]

View 1NNC in 3D

Proteopedia, because life has more than 2D. On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1NNC

Protein Explorer, Easier to use and more powerful than RasMol. (Win and Mac only) Cartoon representation from PDB Cartoon Ramachandran plot from PDBSum

Structure-derived information

Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1NNC, from MSDmotif at EBI Genome occurence of 1NNC's fold from GeneCensus Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1nnc__, region [Jmol] [rasmolscript] [script source] Fold representative 1nnc from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1nnc_A]

Other resources with information on 1NNC

InterPro: IPR001860 MMDB (Entrez's Structure Database)

Movements, Movies and Images

Images from IMB Jena Image Library of Biological Macromolecules.

You may enter another PDB ID code

Go [Back], to the [PDB Lite page], to the [OCA Search page] or to the [PDB Home page]

---

OCA© by Jaime Prilusky, 1996-2007
Bioinformatics and Biological Computing
Weizmann Institute of Science

---