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Structure paper

TitleNarrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase
Journal, issue, pagesBiochemistry, Vol. 43, Page 12780-12787, Year 2004
Publish dateJun 14, 2004 (structure data deposition date)
AuthorsChow, M.A. / McElroy, K.E. / Corbett, K.D. / Berger, J.M. / Kirsch, J.F.
External linksBiochemistry / PubMed:15461450
MethodsX-ray diffraction
Resolution1.85 - 2.31 Å
Structure data

PDB-1toe:
Unliganded structure of Hexamutant + A293D mutant of E. coli aspartate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1tog:
Hydrocinnamic acid-bound structure of SRHEPT + A293D mutant of E. coli aspartate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-1toi:
Hydrocinnamic acid-bound structure of Hexamutant + A293D mutant of E. coli aspartate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1toj:
Hydrocinnamic acid-bound structure of SRHEPT mutant of E. coli aspartate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1tok:
Maleic acid-bound structure of SRHEPT mutant of E. coli aspartate aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-HCI:
HYDROCINNAMIC ACID

ChemComp-MAE:
MALEIC ACID

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / aspartate aminotransferase hexamutant / SRHEPT

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