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PDBe Entry: 1akb view

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING ITS PYRIDOXAL-5'-PHOSPHATE-BINDING LYSINE RESIDUE
Summary
Header TRANSFERASE(AMINOTRANSFERASE)search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 17.8%, Spacegroup: C 2 2 21
Released 31/07/1994, deposition: 28/02/1994, last revision: 24/02/2009
Authors Malashkevich, V.N.search; Jansonius, J.N.search
Primary citation Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
BIOCHEMISTRYsearch vol:34, pag:405-414 (1995) [PubMed ID 7819232 ]search
Keywords TRANSFERASE(AMINOTRANSFERASE)search
EC 2.6.1.1 ExPASy BRENDA search (A)
Organism Gallus gallus(chicken) 9031search(A)
UniProt Aspartate aminotransferase, mitochondrial precursor (EC 2.6.1.1) (Transaminase A) (Glutamate oxaloacetate transaminase 2) P00508search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A ASPARTATE AMINOTRANSFERASE Protein P00508 (AATM_CHICK)search
401 100%
Heterogens
Id Name Ligands
A 2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYLENE)-AMINO]-SUCCINIC ACID PPD search
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