1iny Summary

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A SIALIC ACID DERIVED PHOSPHONATE ANALOG INHIBITS DIFFERENT STRAINS OF INFLUENZA VIRUS NEURAMINIDASE WITH DIFFERENT EFFICIENCIES

The structure was published by White, C.L., Janakiraman, M.N., Laver, W.G., et al., Vasella, A., Air, G.M., and Luo, M., in 1995 in a paper entitled "A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1994.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of INFLUENZA A SUBTYPE N9 NEURAMINIDASE. This molecule has the UniProt identifier P03472 (NRAM_I75A5)search. The sample contained 388 residues which is < 90% of the natural sequence. Out of 388 residues 388 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A INFLUENZA A SUBTYPE N9 NEURAMINIDASE P03472 (83-470) (NRAM_I75A5)search Influenza A virus (A/tern/Australia/G70C/1975(H11N9))search < 90% 388 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P03472 (83 - 470) INFLUENZA A SUBTYPE N9 NEURAMINIDASE Influenza A virus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Sialidases (neuraminidases)search Neuraminidasesearch Neuraminidasesearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P03472) host cell membranesearch membranesearch virion membranesearch carbohydrate metabolic processsearch exo-alpha-sialidase activitysearch

Chain InterPro annotation
A Glycoside hydrolase, family 34search Sialidasessearch