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PDBe Entry: 1aia view

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING THE PYRIDOXAL-5'-PHOSPHATE BINDING LYSINE RESIDUE
Summary
Header TRANSFERASE(AMINOTRANSFERASE)search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 21.0%, Spacegroup: P 1 21 1
Released 15/10/1994, deposition: 10/05/1994, last revision: 24/02/2009
Authors Jaeger, J.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 B)
Organism Escherichia coli 562search(A B)
UniProt Aspartate aminotransferase (EC 2.6.1.1) (ASPAT) (Transaminase A) P00509search (A B)
Polymers
Id Name Type UniProt Residues Observed
A, B ASPARTATE AMINOTRANSFERASE Protein P00509 (AAT_ECOLI)search
396 100%
Heterogens
Id Name Ligands
A, B 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE PMP search
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