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http://purl.uniprot.org/citations/1931125http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1931125http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1931125http://www.w3.org/2000/01/rdf-schema#comment"The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.org/dc/terms/identifier"doi:10.1002/jmr.300040102"xsd:string
http://purl.uniprot.org/citations/1931125http://purl.org/dc/terms/identifier"doi:10.1002/jmr.300040102"xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Bolognesi M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Bolognesi M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Rizzi M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Rizzi M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Coda A."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Coda A."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Mattevi A."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Mattevi A."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Ascenzi P."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Ascenzi P."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Brunori M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Brunori M."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Gatti G."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/author"Gatti G."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/name"J. Mol. Recognit."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/name"J. Mol. Recognit."xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/pages"1-6"xsd:string
http://purl.uniprot.org/citations/1931125http://purl.uniprot.org/core/pages"1-6"xsd:string