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Structure paper

TitleConserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.
Journal, issue, pagesBiochemistry, Vol. 43, Page 1213-1222, Year 2004
Publish dateDec 30, 2003 (structure data deposition date)
AuthorsSandmark, J. / Eliot, A.C. / Famm, K. / Schneider, G. / Kirsch, J.F.
External linksBiochemistry / PubMed:14756557
MethodsX-ray diffraction
Resolution1.71 - 2.42 Å
Structure data

PDB-1s06:
Crystal Structure of the R253K Mutant of 7,8-Diaminopelargonic Acid Synthase
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1s07:
Crystal Structure of the R253A Mutant of 7,8-Diaminopelargonic Acid Synthase
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

PDB-1s08:
Crystal Structure of the D147N Mutant of 7,8-Diaminopelargonic Acid Synthase
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1s09:
Crystal Structure of the Y144F Mutant of 7,8-Diaminopelargonic Acid Synthase
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

PDB-1s0a:
Crystal Structure of the Y17F Mutant of 7,8-Diaminopelargonic Acid Synthase
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Aminotransferase / Fold type I / subclass II / homodimer

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