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http://purl.uniprot.org/SHA-384/3D0367C3ADE50225AF765F6E698BD5D2DF14D021822D8D8BAE17A7827CB41F88F8A1C60290B1AC498EC030EEC7E13075http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/3D0367C3ADE50225AF765F6E698BD5D2DF14D021822D8D8BAE17A7827CB41F88F8A1C60290B1AC498EC030EEC7E13075http://www.w3.org/2000/01/rdf-schema#comment"The GluN1 ligand-binding domain (LBD) showed clear signals corresponding to each of the three N-glycans and indicated the reducing end of glycans at N440 and N771 potentially contacted nearby amino acids. Molecular dynamics simulations identified contacts between nearby amino acids and the N440- and N771-glycans. The distal portions of the N771-glycan also contacted the core residues of the nearby N471-glycan."xsd:string
http://purl.uniprot.org/uniprot/#_542C2BBA8D99C72226E3F623A6E143D93BC7FA73ED57AC641B053A429FAB95B1E0E64D99699D321DF8A1D7E27C30B81Chttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/3D0367C3ADE50225AF765F6E698BD5D2DF14D021822D8D8BAE17A7827CB41F88F8A1C60290B1AC498EC030EEC7E13075
http://purl.uniprot.org/uniprot/Q5VSF9http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/3D0367C3ADE50225AF765F6E698BD5D2DF14D021822D8D8BAE17A7827CB41F88F8A1C60290B1AC498EC030EEC7E13075
http://purl.uniprot.org/uniprot/#_Q5VSF9-mappedCitation-30482728http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/3D0367C3ADE50225AF765F6E698BD5D2DF14D021822D8D8BAE17A7827CB41F88F8A1C60290B1AC498EC030EEC7E13075