2aat | pdb_00002aat

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

spinqualitylabelsall models 2aat, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2aat is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PMP, SO4 Activity: Aspartate transaminase, with EC number 2.6.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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. 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.,Smith DL, Almo SC, Toney MD, Ringe D Biochemistry. 1989 Oct 3;28(20):8161-7. PMID:2513875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate aminotransferase 3D structures

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