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1QIS

ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191F MUTATION, WITH BOUND MALEATE

Summary for 1QIS
Entry DOI10.2210/pdb1qis/pdb
Related1QIR 1QIT
DescriptorASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, MALEIC ACID, ... (4 entities in total)
Functional Keywordsaminotransferase, transferase(aminotransferase), pyridoxal phosphate, maleate
Biological sourceESCHERICHIA COLI
Cellular locationCytoplasm: P00509
Total number of polymer chains1
Total formula weight44026.46
Authors
Jeffery, C.J.,Gloss, L.M.,Petsko, G.A.,Ringe, D. (deposition date: 1999-06-15, release date: 2000-06-05, Last modification date: 2023-12-13)
Primary citationJeffery, C.J.,Gloss, L.M.,Petsko, G.A.,Ringe, D.
The Role of Residues Outside the Active Site in Catalysis: Structural Basis for Function of C191 Mutants of E. Coli Aspartate Aminotransferase
Protein Eng., 13:105-, 2000
Cited by
PubMed: 10708649
DOI: 10.1093/PROTEIN/13.2.105
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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