ChannelsDB: database of biomacromolecular tunnels and pores
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
29036719
PubMed Central
PMC5753359
DOI
10.1093/nar/gkx868
PII: 4316099
Knihovny.cz E-zdroje
- MeSH
- aminokyseliny chemie metabolismus MeSH
- cytochrom P-450 CYP2D6 chemie genetika metabolismus MeSH
- databáze proteinů * MeSH
- eukaryotické buňky cytologie enzymologie MeSH
- exprese genu MeSH
- hydrofobní a hydrofilní interakce MeSH
- iontové kanály chemie genetika metabolismus MeSH
- jaderný pór chemie genetika metabolismus MeSH
- katalytická doména MeSH
- koenzymy chemie metabolismus MeSH
- lidé MeSH
- mutace MeSH
- prokaryotické buňky cytologie enzymologie MeSH
- software * MeSH
- statická elektřina MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aminokyseliny MeSH
- cytochrom P-450 CYP2D6 MeSH
- iontové kanály MeSH
- koenzymy MeSH
ChannelsDB (http://ncbr.muni.cz/ChannelsDB) is a database providing information about the positions, geometry and physicochemical properties of channels (pores and tunnels) found within biomacromolecular structures deposited in the Protein Data Bank. Channels were deposited from two sources; from literature using manual deposition and from a software tool automatically detecting tunnels leading to the enzymatic active sites and selected cofactors, and transmembrane pores. The database stores information about geometrical features (e.g. length and radius profile along a channel) and physicochemical properties involving polarity, hydrophobicity, hydropathy, charge and mutability. The stored data are interlinked with available UniProt annotation data mapping known mutation effects to channel-lining residues. All structures with channels are displayed in a clear interactive manner, further facilitating data manipulation and interpretation. As such, ChannelsDB provides an invaluable resource for research related to deciphering the biological function of biomacromolecular channels.
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