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Structure paper

TitleThe role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
Journal, issue, pagesProtein Eng., Vol. 13, Page 105-112, Year 2000
Publish dateDec 30, 1998 (structure data deposition date)
AuthorsJeffery, C.J. / Gloss, L.M. / Petsko, G.A. / Ringe, D.
External linksProtein Eng. / PubMed:10708649
MethodsX-ray diffraction
Resolution1.9 - 2.45 Å
Structure data

PDB-1b4x:
ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

PDB-1qir:
ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191Y MUTATION, WITH BOUND MALEATE
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1qis:
ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191F MUTATION, WITH BOUND MALEATE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1qit:
ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191W MUTATION, WITH BOUND MALEATE
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5eaa:
ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-MAE:
MALEIC ACID

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / AMINOTRANSFERASE / TRANSFERASE(AMINOTRANSFERASE) / PYRIDOXAL PHOSPHATE / MALEATE

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