Crystal Structure of the R253A Mutant of 7,8-Diaminopelargonic Acid Synthase

Summary for 1S07

Related1qj5 1dty 1qj3 1mly 1mlz 1mgv 1S06 1S08 1S09 1S0A
DescriptorAdenosylmethionine-8-amino-7-oxononanoate aminotransferase, SODIUM ION, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total)
Functional Keywordsaminotransferase, fold type i, subclass ii, homodimer, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm (By similarity) P12995
Total number of polymer chains2
Total molecular weight95048.91
Sandmark, J.,Eliot, A.C.,Famm, K.,Schneider, G.,Kirsch, J.F. (deposition date: 2003-12-30, release date: 2004-03-23, Last modification date: 2011-07-13)
Primary citation
Sandmark, J.,Eliot, A.C.,Famm, K.,Schneider, G.,Kirsch, J.F.
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.
Biochemistry, 43:1213-1222, 2004
PubMed: 14756557 (PDB entries with the same primary citation)
DOI: 10.1021/bi0358059
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.23290.8%3.4%3.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution