5MTC
Crystal structure of PDF from the Vibrio parahaemolyticus bacteriophage VP16T - crystal form I
Summary for 5MTC
Entry DOI | 10.2210/pdb5mtc/pdb |
Descriptor | Putative uncharacterized protein orf60T, ZINC ION, NICKEL (II) ION, ... (4 entities in total) |
Functional Keywords | pdf, peptide deformylase, type 1b, bacteriophage vp16t, hydrolase |
Biological source | Vibrio phage VP16T |
Total number of polymer chains | 2 |
Total formula weight | 29856.76 |
Authors | Fieulaine, S.,Grzela, R.,Giglione, C.,Meinnel, T. (deposition date: 2017-01-09, release date: 2017-09-20, Last modification date: 2024-01-17) |
Primary citation | Grzela, R.,Nusbaum, J.,Fieulaine, S.,Lavecchia, F.,Bienvenut, W.V.,Dian, C.,Meinnel, T.,Giglione, C. The C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation. Sci Rep, 7:11041-11041, 2017 Cited by PubMed: 28887476DOI: 10.1038/s41598-017-11329-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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