RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23871710http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23871710http://www.w3.org/2000/01/rdf-schema#comment"Crystallographic analysis of a mutated form of "loopful" GH19 chitinase from rye seeds a double mutant RSC-c, in which Glu67 and Trp72 are mutated to glutamine and alanine, respectively, (RSC-c-E67Q/W72A) in complex with chitin tetrasaccharide (GlcNAc)₄ revealed that the entire substrate-binding cleft was completely occupied with the sugar residues of two (GlcNAc)₄ molecules. One (GlcNAc)₄ molecule bound to subsites -4 to -1, while the other bound to subsites +1 to +4. Comparisons of the main chain conformation between liganded RSC-c-E67Q/W72A and unliganded wild type RSC-c suggested domain motion essential for catalysis. This is the first report on the complete subsite mapping of GH19 chitinase."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2013.07.008"xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/author"Kondo K."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/author"Numata T."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/author"Fukamizo T."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/author"Ohnuma T."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/author"Umemoto N."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/pages"2691-2697"xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/title"Complete subsite mapping of a "loopful" GH19 chitinase from rye seeds based on its crystal structure."xsd:string
http://purl.uniprot.org/citations/23871710http://purl.uniprot.org/core/volume"587"xsd:string
http://purl.uniprot.org/citations/23871710http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23871710
http://purl.uniprot.org/citations/23871710http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23871710
http://purl.uniprot.org/uniprot/#_Q9FRV0-mappedCitation-23871710http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23871710
http://purl.uniprot.org/uniprot/Q9FRV0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23871710