1S06

Crystal Structure of the R253K Mutant of 7,8-Diaminopelargonic Acid Synthase

Summary for 1S06

Related1qj5 1dty 1qj3 1mly 1mlz 1mgv 1S07 1S08 1S09 1S0A
DescriptorAdenosylmethionine-8-amino-7-oxononanoate aminotransferase, SODIUM ION (3 entities in total)
Functional Keywordsaminotransferase, fold type i, subclass ii, homodimer, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm  P12995
Total number of polymer chains2
Total molecular weight95066.96
Authors
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: 2018-01-31)
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
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.23280.7%4.1%2.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution