1AHY: Aspartate Aminotransferase Hexamutant

Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands.
PDB ID: 1AHYDownload
MMDB ID: 3768
PDB Deposition Date: 1995/2/21
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1AHY: dimeric; determined by author and by software (PISA)
Molecular Components in 1AHY
Label Count Molecule
Proteins (2 molecules)
Aspartate Aminotransferase(Gene symbol: aspC)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB