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1S06

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

Summary for 1S06
Entry DOI10.2210/pdb1s06/pdb
Related1S07 1S08 1S09 1S0A 1dty 1mgv 1mly 1mlz 1qj3 1qj5
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 formula 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: 2024-04-03)
Primary citationSandmark, 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
Cited by
PubMed: 14756557
DOI: 10.1021/bi0358059
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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