PDBe-KB: a community-driven resource for structural and functional annotations
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F20%3A73604175" target="_blank" >RIV/61989592:15310/20:73604175 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11320/19:10407730 RIV/00216224:14740/20:00117896
Result on the web
<a href="https://academic.oup.com/nar/article/48/D1/D344/5580911" target="_blank" >https://academic.oup.com/nar/article/48/D1/D344/5580911</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkz853" target="_blank" >10.1093/nar/gkz853</a>
Alternative languages
Result language
angličtina
Original language name
PDBe-KB: a community-driven resource for structural and functional annotations
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA17-21122S" target="_blank" >GA17-21122S: MolMeDB - Validated Predictions of Small Molecule Interactions with Biological Membranes</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
NUCLEIC ACIDS RESEARCH
ISSN
0305-1048
e-ISSN
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Volume of the periodical
48
Issue of the periodical within the volume
D1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
344-353
UT code for WoS article
000525956700048
EID of the result in the Scopus database
2-s2.0-85075918849