2aat: Difference between revisions

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[[Image:2aat.jpg|left|200px]]
{{Seed}}
[[Image:2aat.png|left|200px]]


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{{STRUCTURE_2aat|  PDB=2aat  |  SCENE=  }}  
{{STRUCTURE_2aat|  PDB=2aat  |  SCENE=  }}  


'''2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI'''
===2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI===




==Overview==
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The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction. The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is compared to that of the mitochondrial aspartate aminotransferase. The most striking differences, aside from the absence of the lysine side chain, occur in the positions of the pyridoxamine group and of tryptophan 140.
The line below this paragraph, {{ABSTRACT_PUBMED_2513875}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 2513875 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2513875}}


==About this Structure==
==About this Structure==
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[[Category: Smith, D.]]
[[Category: Smith, D.]]
[[Category: Toney, M.]]
[[Category: Toney, M.]]
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