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Title: PROCOGNATE: a cognate ligand domain mapping for enzymes

Journal Article · · Nucleic Acids Research
DOI:https://doi.org/10.1093/nar/gkm611· OSTI ID:1625427
 [1];  [2];  [1]
  1. European Molecular Biology Lab. (EMBL), Cambridge (United Kingdom). Wellcome Trust Genome Campus
  2. King's College, London (United Kingdom). Randall Division of Cell and Molecular Biophysics

PROCOGNATE is a database of protein cognate ligands for the domains in enzyme structures as described by CATH, SCOP and Pfam, and is available as an interactive website or a flat file. This article gives an overview of the database and its generation and presents a new website front end, as well as recent increased coverage in our dataset via inclusion of Pfam domains. We also describe navigation of the website and its features. The current version (1.3) of PROCOGNATE covers 4123, 4536, 5876 structures and 377, 326, 695 superfamilies/families in CATH, SCOP and Pfam, respectively. PROCOGNATE can be accessed at: http://www.ebi.ac.uk/ thornton-srv/databases/procognate/

Research Organization:
European Molecular Biology Lab. (EMBL), Cambridge (United Kingdom)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division; National Institutes of Health (NIH)
Grant/Contract Number:
W-31-109-ENG38; GM62414
OSTI ID:
1625427
Journal Information:
Nucleic Acids Research, Vol. 36, Issue suppl_1; ISSN 0305-1048
Publisher:
Oxford University PressCopyright Statement
Country of Publication:
United States
Language:
English

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Systematic domain-based aggregation of protein structures highlights DNA-, RNA-, and other ligand-binding positions posted_content August 2018
IsoCleft Finder – a web-based tool for the detection and analysis of protein binding-site geometric and chemical similarities journal January 2013
iPfam: a database of protein family and domain interactions found in the Protein Data Bank journal December 2013
Characterizing the pocketome of Mycobacterium tuberculosis and application in rationalizing polypharmacological target selection journal September 2014
Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently journal January 2015
The Phylogenomic Roots of Modern Biochemistry: Origins of Proteins, Cofactors and Protein Biosynthesis journal January 2012
Protein Conformational Diversity Modulates Sequence Divergence journal March 2012
PepX: a structural database of non-redundant protein–peptide complexes journal October 2009
SuperSite: dictionary of metabolite and drug binding sites in proteins journal January 2009
@TOME-2: a new pipeline for comparative modeling of protein-ligand complexes journal May 2009
firestar —advances in the prediction of functionally important residues journal June 2011
Identification of NAD interacting residues in proteins journal March 2010
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FLORA: A Novel Method to Predict Protein Function from Structure in Diverse Superfamilies journal August 2009
Combinatorial Clustering of Residue Position Subsets Predicts Inhibitor Affinity across the Human Kinome journal June 2013
Prediction of Detailed Enzyme Functions and Identification of Specificity Determining Residues by Random Forests journal January 2014

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