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http://purl.uniprot.org/SHA-384/A54E3C474990D2111216C5669EFCEB604A2B7DDC92A7872E4A574B2961EC8128CD021589C49672F1CBD70574A8B8F82Chttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/A54E3C474990D2111216C5669EFCEB604A2B7DDC92A7872E4A574B2961EC8128CD021589C49672F1CBD70574A8B8F82Chttp://www.w3.org/2000/01/rdf-schema#comment"results from molecular dynamics studies show dynamics of Pin1 and the enzyme-substrate interactions are intricately coupled to isomerization during catalysis; strength of interactions between phosphate binding pocket of Pin1 and the phosphate moiety of the substrate is dictated by the state of the substrate during catalysis"xsd:string
http://purl.uniprot.org/uniprot/#_3BF1227B512ECB735B33173C1379ADF4002071684AF0AF7D37BB82BDD16EC701A44C68F85B4575EFF77D743E33981C02http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/A54E3C474990D2111216C5669EFCEB604A2B7DDC92A7872E4A574B2961EC8128CD021589C49672F1CBD70574A8B8F82C
http://purl.uniprot.org/uniprot/Q8NFL2http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/A54E3C474990D2111216C5669EFCEB604A2B7DDC92A7872E4A574B2961EC8128CD021589C49672F1CBD70574A8B8F82C
http://purl.uniprot.org/uniprot/#_Q8NFL2-mappedCitation-23980573http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/A54E3C474990D2111216C5669EFCEB604A2B7DDC92A7872E4A574B2961EC8128CD021589C49672F1CBD70574A8B8F82C