All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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