1 - 13 of 13 results

SugarBindDB / SugarBind Database

Covers knowledge of glycan binding of human pathogen lectins and adhesins. SugarBindDB is a curated database; each glycan-protein binding pair is associated with at least one published reference. The core data element of SugarBindDB is a set of three inseparable components: the pathogenic agent, a lectin/adhesin and a glycan ligand. Each entity (agent, lectin or ligand) is described by a range of properties that are summarized in an entity-dedicated page. Several search, navigation and visualisation tools are implemented to investigate the functional role of glycans in pathogen binding. The database is cross-linked to protein and glycan-related resources such as UniProtKB and UniCarbKB.

EK3D / E. coli K antigen 3-Dimensional Structure Database

A repository of 72 E. coli K antigens that provides information about sugar compositions, their anomeric and enantiomeric forms and linkages between the sugar monomers. The database also has the collection of 3D structural models of the K antigen repeating units that are derived from the above information. As the classification of E. coli into group 1, 2, 3 and 4 is developed based on K antigens, the database also contains information about the group based serotyping of E. coli K antigens. As the capsules are molecules of 100–10000 kD multimers, the database also provides the facility to generate polymeric structures of K antigen repeat units.


Assists data interpretation to bring glycan analysis within the reach of any well-established laboratory. GlycoBase provides an open-access relational database of glycan structures and primary research data, accessed via a web-based interface. It was designed to support HILIC 2-aminobenzamide (2AB) approaches with an open-source philosophy intended to enhance software development, data management, and to progress the application of glycoinformatics in glycomics and glycoproteomics.


A mass spectrometry-based glycoproteomic characterization of zebrafish embryos was performed to identify the N-linked glycoproteins and N-linked glycosylation sites. To increase the number of glycopeptides, proteins from zebrafish were digested with two different proteases--chymotrypsin and trypsin--into peptides of different length. The N-glycosylated peptides of zebrafish were then captured by the solid-phase extraction of N-linked glycopeptides (SPEG) method and the peptides were identified with an LTQ OrbiTrap Velos mass spectrometer.


Provides a list of all available experimental information on agl (archaeal glycosylation) genes and proteins. Aglgenes offers a web interface that does not requires any particular training. It includes a single search field that allows user to search through all published experimental data on genes and proteins involved in archaeal N-glycosylation. This database allows users to submit updates on existing entries or new information on archaeal N-glycosylation pathway components.