1hfk | pdb_00001hfk

Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate

spinqualitylabelsall models 1hfk, resolution 2.17Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1hfk is a 2 chain structure with sequence from Dickeya chrysanthemi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.17Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ASPG_DICCH Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance. Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.,Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Asparaginase 3D structures

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