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http://purl.uniprot.org/SHA-384/740170923AF77109DF01A95E3E01C7EE0C6CBB2F87C7892E77E2F6A01A0B8135E21C923A86DA5F57A263C3A9B792F06Chttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/740170923AF77109DF01A95E3E01C7EE0C6CBB2F87C7892E77E2F6A01A0B8135E21C923A86DA5F57A263C3A9B792F06Chttp://www.w3.org/2000/01/rdf-schema#comment"Study solves the crystal structure of an ATP-bound wild-type human ABCF1 at 2.3-A resolution. The comparative studies indicate that the structure is in a pre-activation intermediate conformation. This conformation is stabilized by the interaction between ATP and protein suggesting that this conformation is an important step in the activation of ABCF1."xsd:string
http://purl.uniprot.org/uniprot/#_35B73740F0964111FAC73C95958D32095A42AF1C9D27DE0B6474C33A4ABE315606216628FF7D991FBD29B226B497C8BDhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/740170923AF77109DF01A95E3E01C7EE0C6CBB2F87C7892E77E2F6A01A0B8135E21C923A86DA5F57A263C3A9B792F06C
http://purl.uniprot.org/uniprot/Q2L6I2http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/740170923AF77109DF01A95E3E01C7EE0C6CBB2F87C7892E77E2F6A01A0B8135E21C923A86DA5F57A263C3A9B792F06C
http://purl.uniprot.org/uniprot/#_Q2L6I2-mappedCitation-30017566http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/740170923AF77109DF01A95E3E01C7EE0C6CBB2F87C7892E77E2F6A01A0B8135E21C923A86DA5F57A263C3A9B792F06C