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Structure paper

TitleThe Structures of Aspartate Aminotransferase with Mutations of Non-Active-Site Residues
Journal, issue, pagesTo be Published
Publish dateNov 8, 2005 (structure data deposition date)
AuthorsTanaka, Y. / Nakagawa, N. / Tada, H. / Yano, T. / Masui, R. / Kuramitsu, S.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.98 - 2.66 Å
Structure data

PDB-2d5y:
Aspartate Aminotransferase Mutant MC With Isovaleric Acid
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

PDB-2d61:
Aspartate Aminotransferase Mutant MA With Maleic Acid
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-2d63:
Aspartate Aminotransferase Mutant MA With Isovaleric Acid
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-2d64:
Aspartate Aminotransferase Mutant MABC With Isovaleric Acid
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-2d65:
Aspartate Aminotransferase Mutant MABC
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2d66:
Aspartate Aminotransferase Mutant MAB
Method: X-RAY DIFFRACTION / Resolution: 2.18 Å

PDB-2d7y:
Aspartate Aminotransferase Mutant MA
Method: X-RAY DIFFRACTION / Resolution: 2.66 Å

PDB-2d7z:
Aspartate Aminotransferase Mutant MAB Complexed with Maleic Acid
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-IVA:
ISOVALERIC ACID

ChemComp-HOH:
WATER

ChemComp-MAE:
MALEIC ACID

ChemComp-SO4:
SULFATE ION

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / aspartate aminotransferase / directed evolution / protein design / protein enginnering / direct evolution

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