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http://purl.uniprot.org/SHA-384/173E49D88C697BDF9196F2EF1DFA86F462BCF19BB3EBCBFDDC46EEEBE62FD21D8BF8A7BDE2602FF5C44739290F7F986Dhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/173E49D88C697BDF9196F2EF1DFA86F462BCF19BB3EBCBFDDC46EEEBE62FD21D8BF8A7BDE2602FF5C44739290F7F986Dhttp://www.w3.org/2000/01/rdf-schema#comment"Taken together these data suggest hat the altered hydrogen bonding observed in the Hsc70 C17W mutant (where the connectivity between Mg2+.nucleotide and E175 is also disrupted) could bring about changes to Hsc70 domain communication affecting peptide association while also limiting ATP hydrolysis."xsd:string
http://purl.uniprot.org/uniprot/#_11B98B6779F252B81D1B955A2A1B7E9999346499543E31C72C3B6A1D90D41C6525925CF91010259D93D3D4FA76FAABDEhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/173E49D88C697BDF9196F2EF1DFA86F462BCF19BB3EBCBFDDC46EEEBE62FD21D8BF8A7BDE2602FF5C44739290F7F986D
http://purl.uniprot.org/uniprot/Q96BE0http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/173E49D88C697BDF9196F2EF1DFA86F462BCF19BB3EBCBFDDC46EEEBE62FD21D8BF8A7BDE2602FF5C44739290F7F986D
http://purl.uniprot.org/uniprot/#_Q96BE0-mappedCitation-29300467http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/173E49D88C697BDF9196F2EF1DFA86F462BCF19BB3EBCBFDDC46EEEBE62FD21D8BF8A7BDE2602FF5C44739290F7F986D