1e8t Summary



The structure was published by Crennell, S., Takimoto, T., Portner, A., and Taylor, G., in 2000 in a paper entitled "Crystal Structure of the Multifunctional Paramyxovirus Hemagglutinin-Neuraminidase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2000.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of HEMAGGLUTININ-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 homodimers.

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 HEMAGGLUTININ-NEURAMINIDASE Q9Q2W5 (124-577) (HN_NDVK)search Newcastle disease virus (strain Kansas)search < 90% 454 99%
B HEMAGGLUTININ-NEURAMINIDASE Q9Q2W5 (124-577) (HN_NDVK)search Newcastle disease virus (strain Kansas)search < 90% 454 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9Q2W5 (124 - 577) HEMAGGLUTININ-NEURAMINIDASE Newcastle disease virus (strain Kansas)

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Sialidases (neuraminidases)search Neuraminidasesearch Haemagglutinin-neuraminidasesearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A, B (Q9Q2W5) viral life cyclesearch viral envelopesearch host cell surface receptor bindingsearch exo-alpha-sialidase activitysearch

Chain InterPro annotation
A, B Haemagglutinin-neuraminidasesearch Sialidasessearch