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http://purl.uniprot.org/citations/6430186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6430186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6430186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/6430186http://www.w3.org/2000/01/rdf-schema#comment"The structure of human erythrocyte carbonic anhydrase I has been refined to a final R value of 19% to 2-A resolution by a combination of least squares refinement and model fitting in a three-dimensional graphics display. About 300 solvent atoms have been located bound to the protein molecule. An interesting hydrogen bond network involving Zn2+, the liganded solvent, side chain groups of Thr-199, Glu-106, Thr-7, and His-64 through two solvent molecules have been found that may be important for the catalytic mechanism of the carbonic anhydrase."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.org/dc/terms/identifier"doi:10.1111/j.1749-6632.1984.tb12314.x"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.org/dc/terms/identifier"doi:10.1111/j.1749-6632.1984.tb12314.x"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.org/dc/terms/identifier"doi:10.1111/j.1749-6632.1984.tb12314.x"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Jones T.A."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Jones T.A."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Kannan K.K."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Kannan K.K."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Ramanadham M."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/author"Ramanadham M."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/date"1984"xsd:gYear
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/name"Ann. N. Y. Acad. Sci."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/name"Ann. N. Y. Acad. Sci."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/pages"49-60"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/pages"49-60"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/title"Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/title"Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I."xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/volume"429"xsd:string
http://purl.uniprot.org/citations/6430186http://purl.uniprot.org/core/volume"429"xsd:string
http://purl.uniprot.org/citations/6430186http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6430186
http://purl.uniprot.org/citations/6430186http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6430186