Tools   Select Another Resource Report Type

http://pcidb.russelllab.org/

The database of protein-chemical structural interactions includes all existing 3D structures of complexes of proteins with low molecular weight ligands. When one considers the proteins and chemical vertices of a graph, all these interactions form a network. Biological networks are powerful tools for predicting undocumented relationships between molecules. The underlying principle is that existing interactions between molecules can be used to predict new interactions. For pairs of proteins sharing a common ligand, we use protein and chemical superimpositions combined with fast structural compatibility screens to predict whether additional compounds bound by one protein would bind the other. The current version includes data from the Protein Data Bank as of August 2011. The database is updated monthly.

Proper citation: ProtChemSI (RRID:SCR_006115) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/

Portal of glycoinformatics resources including databases and bioinformatics tools for glycobiology and glycomics research. Databases include a bibliography, structure, nuclear magnetic resonance (NMR), mass spectroscopy (ms) and a PDB search.

Proper citation: glycosciences.de (RRID:SCR_002324) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/modeling/pdb2mgif/

A web tool that takes a 3D structure (a PDB input file) and generates an animated image which can be displayed using any browser without the need for any additional molecular visualization software.

Proper citation: PDB2MultiGif (RRID:SCR_001489) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/modeling/glyprot/

Web-based tool that enables meaningful N-glycan conformations to be attached to all the spatially accessible potential N-glycosylation sites of a known three-dimensional (3D) protein structure. The 3D structure of protein is required as input. Potential N-glysylations site are automatically detected. The attached glycan are constructed with SWEET-II, http://www.glycosciences.de/modeling/sweet2/doc/index.php

Proper citation: GlyProt (RRID:SCR_001560) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/tools/pdbcare/

Tool that checks carbohydrate residues in pdb-files for errors, aiding experimentalists in detecting discrepancies in connectivities and nomenclature.

Proper citation: pdb-care (RRID:SCR_001562) Copy   

•   Source: SciCrunch Registry

http://www.ebi.ac.uk/pdbsum

Pictorial database of an at-a-glance overview of the contents of each 3D structure deposited in the Protein Data Bank (PDB). It shows the molecule(s) that make up the structure (ie protein chains, DNA, ligands and metal ions) and schematic diagrams of their interactions. Extensive use is made of the freely available RasMol molecular graphics program to view the molecules and their interactions in 3D. Entries are accessed either by their 4-character PDB code, or by one of the two search boxes provided on the PDBsum home page: text search or sequence search. The information given on each PDBsum entry is spread across several pages, as listed below and accessible from the tabs at the top of the page. Only the relevant tabs will be present on any given page. * Top page - summary information including thumbnail image of structure, molecules in structure, enzyme reaction diagram (where relevant), GO functional assignments, and selected figures from key reference * Protein - wiring diagram, topology diagram(s) by CATH domain, and residue conservation (where available) * DNA/RNA - DNA/RNA sequence and NUCPLOT showing interactions made with protein * Ligands - description of bound molecule and LIGPLOT showing interactions made with protein * Prot-prot - schematic diagrams of any protein-protein interfaces and the residue-residue interactions made across them * Clefts - listing of top ten clefts in the surface of the protein, listed by volume with any bound ligands shown * Links - links to external databases Additionally, it accepts users'''' own PDB format files and generates a private set of analyses for each uploaded structure.

Proper citation: PDBsum (RRID:SCR_006511) Copy   

•   Source: SciCrunch Registry

http://www.thesgc.org/

Charity registered in United Kingdom whose mission is to accelerate research in new areas of human biology and drug discovery.Not for profit, public-private partnership that carries out basic science of relevance to drug discovery whose core mandate is to determine 3D structures on large scale and cost effectively targeting human proteins of biomedical importance and proteins from human parasites that represent potential drug targets.

Proper citation: Structural Genomics Consortium (RRID:SCR_003890) Copy   

•   Source: SciCrunch Registry

http://www.glycosciences.de/tools/carp/

Service that generates Ramachandran-like plots of carbohydrate linkage torsions in pdb-files. The Ramachandran Plot, where backbone torsion angles are plotted against each other, is a frequently used tool to evaluate the quality of a protein 3D structure. For carbohydrate structures, linkage torsions can be evaluated in a similar way. Preferred Phi/Psi values of the torsion angles of glycosidic bonds depend strongly on the types of monosaccharides involved in the linkage, the kind of linkage (1-3, 1-4, etc) as well as the degree of branching of the structure. CARP analyses carbohydrate data given in PDB files using the pdb2linucs algorithm. For each different linkage type a separate plot is generated. The user can choose between two sources for plot background information for comparison: data obtained from PDB provided by GlyTorsion or from GlycoMapsDB. GlycoMapsDB provides calculated conformational maps, which show energetically preferred regions for a specific linkage, while PDB data are based on experimentally solved structures. For seldom occuring linkages, however, PDB data are often rare, so maybe not sufficient background information for comparison will be available from this source., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.

Proper citation: CARP (RRID:SCR_009021) Copy   

•   Source: SciCrunch Registry