2aat
From Proteopedia
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI
Overview
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.
About this Structure
2AAT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 23 14:36:00 2008
