3BFP
Crystal Structure of apo-PglD from Campylobacter jejuni
Summary for 3BFP
Entry DOI | 10.2210/pdb3bfp/pdb |
Related | 2VHE |
Descriptor | Acetyltransferase, CITRATE ANION (3 entities in total) |
Functional Keywords | left-handed beta helix, n-acetyltransferase, coa binding protein, n-glycan biosynthesis, bacillosamine, structural genomics, mkbsgi, montreal-kingston bacterial structural genomics initiative, bsgi, transferase |
Biological source | Campylobacter jejuni |
Total number of polymer chains | 1 |
Total formula weight | 21232.65 |
Authors | Rangarajan, E.S.,Watson, D.C.,Leclerc, S.,Proteau, A.,Cygler, M.,Matte, A.,Young, N.M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2007-11-22, release date: 2008-01-22, Last modification date: 2024-02-21) |
Primary citation | Rangarajan, E.S.,Ruane, K.M.,Sulea, T.,Watson, D.C.,Proteau, A.,Leclerc, S.,Cygler, M.,Matte, A.,Young, N.M. Structure and Active Site Residues of PglD, an N-Acetyltransferase from the Bacillosamine Synthetic Pathway Required for N-Glycan Synthesis in Campylobacter jejuni. Biochemistry, 47:1827-1836, 2008 Cited by PubMed: 18198901DOI: 10.1021/bi702032r PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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