2jkb Summary



The structure was published by Gut, H., King, S.J., and Walsh, M.A., in 2008 in a paper entitled "Structural and Functional Studies of Streptococcus Pneumoniae Neuraminidase B: An Intramolecular Trans-Sialidase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.54 Å and deposited in 2008.

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

The PDB entry contains the structure of SIALIDASE B.

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 B Q54727 (30-697) (NANB_STRPN)search Streptococcus pneumoniae TIGR4search 100% 686 96%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q54727 (30 - 697) SIALIDASE B Streptococcus pneumoniae TIGR4

Chain Structural classification (CATH) Sequence family (Pfam)
A (Q54727) Neuraminidasesearch, Intramolecular Trans-sialidase; Domain 3search PF02012: BNR/Asp-box repeatsearch, PF02973: Sialidase, N-terminal domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (Q54727) exo-alpha-sialidase activitysearch exo-alpha-(2->3)-sialidase activitysearch exo-alpha-(2->6)-sialidase activitysearch hydrolase activity, acting on glycosyl bondssearch exo-alpha-(2->8)-sialidase activitysearch hydrolase activitysearch carbohydrate metabolic processsearch metabolic processsearch

Chain InterPro annotation
A BNR repeatsearch Glycoside hydrolase, family 33, N-terminalsearch search Sialidasessearch Concanavalin A-like lectin/glucanase domainsearch Trans-sialidase, domain 3search