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http://purl.uniprot.org/citations/1567418http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1567418http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1567418http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys blomhoffii has been determined by molecular replacement methods based on the known structure of Crotalus atrox PLA2, a same group II enzyme. The overall structures, except the calcium-binding regions, are very similar to each other. A calcium ion is pentagonally ligated to two carboxylate oxygen atoms of Asp-49 and each carbonyl oxygen atoms of Tyr-28, Gly-30 and Ala-31. A reason why the former enzyme functions as monomeric form, while the latter one does as dimer, could be presumed by the structural comparison of these calcium-binding regions. Although Gly-32 is usually participated as a ligand in the coordination with calcium ion in group I PLA2, it is characteristically replaced to Ala-31 in the present structure, and thus the coordination geometry of calcium ion is rather different from the usually observed one."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.org/dc/terms/identifier"doi:10.1016/0006-291x(92)91169-q"xsd:string
http://purl.uniprot.org/citations/1567418http://purl.org/dc/terms/identifier"doi:10.1016/0006-291x(92)91169-q"xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Hata Y."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Hata Y."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ishida T."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ishida T."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ikeda K."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ikeda K."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Inoue M."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Inoue M."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Samejima Y."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Samejima Y."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Tomoo K."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Tomoo K."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Doi M."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Doi M."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ohishi H."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/author"Ohishi H."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/1567418http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string