3beq Summary

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Neuraminidase of A/Brevig Mission/1/1918 H1N1 strain

The structure was published by Xu, X., Zhu, X., Dwek, R.A., Stevens, J., and Wilson, I.A., in 2008 in a paper entitled "Structural characterization of the 1918 influenza virus H1N1 neuraminidase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.64 Å and deposited in 2007.

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

This PDB entry contains multiple copies of the structure of Neuraminidase.

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 Neuraminidase Q9IGQ6 (83-467) (NRAM_I18A0)search Influenza A virus (A/Brevig Mission/1/1918(H1N1))search < 90% 385 100%
B Neuraminidase Q9IGQ6 (83-467) (NRAM_I18A0)search Influenza A virus (A/Brevig Mission/1/1918(H1N1))search < 90% 385 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9IGQ6 (83 - 467) Neuraminidase Influenza A virus

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Neuraminidasesearch Neuraminidasesearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (Q9IGQ6) host cell membranesearch virion membranesearch membranesearch exo-alpha-sialidase activitysearch carbohydrate metabolic processsearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 34search Sialidasessearch