PDBe-KB: a community-driven resource for structural and functional annotations
| Autoři |
VARADI Mihaly
BCRRISFORD John
DESHPANDE Mandar
NAIR Sreenath S.
GUTMANAS Aleksandras
ARMSTRONG David
PRAVDA Lukáš
AL-LAZIKANI Bissan
ANYANGO Stephen
BARTON Geoffrey J.
BERKA Karel
BLUNDELL Tom
BORKAKOTI Neera
DANA Jose
DAS Sayoni
DEY Sucharita
DI MICCO Patrizio
FRATERNALI Franca
GIBSON Toby
HELMER-CITTERICH Manuela
HOKSZA David
HUANG Liang-Chin
JAIN Rishabh
JUBB Harry
KANNAS Christos
KANNAN Natarajan
KOČA Jaroslav
KRIVAK Radoslav
KUMAR Manjeet
LEVY Emanuel D.
MADEIRA F.
MADHUSUDHAN M. S.
MARTELL Henry J.
MACGOWAN Stuart
MCGREIG Jake E.
MIR Saqib
MUKHOPADHYAY Abhik
PARCA Luca
PAYSAN-LAFOSSE Typhaine
RADUSKY Leandro
RIBEIRO Antonio
SERRANO Luis
SILLITOE Ian
SINGH Gulzar
SKODA Petr
SVOBODOVÁ Radka
TYZACK Jonathan
VALENCIA Alfonso
FERNANDEZ Eloy Villasclaras
VRANKEN Wim
WASS Mark
THORNTON Janet
STERNBERG Michael
ORENGO Christine
VELANKAR Sameer
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| Rok publikování |
2020 |
| Druh |
Článek v odborném periodiku
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| Časopis / Zdroj |
Nucleic acids research |
| Fakulta / Pracoviště MU |
Středoevropský technologický institut
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| Citace |
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| www |
https://doi.org/10.1093/nar/gkz853
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| Doi |
http://dx.doi.org/10.1093/nar/gkz853 |
| Klíčová slova |
PDBe-KB
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| Popis |
The Protein Data Bank in Europe-Knowledge Base (PDBe-KB, https://pdbe-kb.org) is a community-driven, collaborative resource for literature-derived, manually curated and computationally predicted structural and functional annotations of macro-molecular structure data, contained in the Protein Data Bank (PDB). The goal of PDBe-KB is two-fold: (i) to increase the visibility and reduce the fragmentation of annotations contributed by specialist data resources, and to make these data more findable, accessible, interoperable and reusable (FAIR) and (ii) to place macromolecular structure data in their biological context, thus facilitating their use by the broader scientific community in fundamental and applied research. Here, we describe the guidelines of this collaborative effort, the current status of contributed data, and the PDBe-KB infrastructure, which includes the data exchange format, the deposition system for added value annotations, the distributable database containing the assembled data, and programmatic access endpoints. We also describe a series of novel web-pages-the PDBe-KB aggregated views of structure data-which combine information on macromolecular structures from many PDB entries. We have recently released the first set of pages in this series, which provide an overview of available structural and functional information for a protein of interest, referenced by a UniProtKB accession.
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