1dim Summary



The structure was published by Crennell, S.J., Garman, E.F., Philippon, C., et al., Laver, W.G., Vimr, E.R., and Taylor, G.L., in 1996 in a paper entitled "The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1996.

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

The PDB entry contains the structure of SIALIDASE. This molecule has the UniProt identifier P29768 (NANH_SALTY)search. The sample contained 381 residues which is 100% of the natural sequence. Out of 381 residues 381 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 is most likely monomeric.

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 SIALIDASE P29768 (2-382) (NANH_SALTY)search Salmonella enterica subsp. enterica serovar Typhimurium str. LT2search 99% 381 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P29768 (2 - 382) SIALIDASE Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P29768) Sialidases (neuraminidases)search Neuraminidasesearch PF02012: BNR/Asp-box repeatsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P29768) exo-alpha-(2->8)-sialidase activitysearch exo-alpha-sialidase activitysearch exo-alpha-(2->3)-sialidase activitysearch exo-alpha-(2->6)-sialidase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch pathogenesissearch metabolic processsearch

Chain InterPro annotation
A Trypanosome sialidasesearch Sialidasessearch Sialidase familysearch