1LM4
Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A
Summary for 1LM4
Entry DOI | 10.2210/pdb1lm4/pdb |
Related | 1LM6 1LME |
Descriptor | peptide deformylase PDF1, FE (III) ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | pdf, metalloenzyme, staphylococcus aureus, hydrolase |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 2 |
Total formula weight | 44137.80 |
Authors | Kreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A. (deposition date: 2002-04-30, release date: 2003-06-24, Last modification date: 2023-11-15) |
Primary citation | Kreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A. Structure analysis of peptide deformylases from streptococcus pneumoniae,staphylococcus aureus, thermotoga maritima, and pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase J.MOL.BIOL., 330:309-321, 2003 Cited by PubMed: 12823970DOI: 10.1016/S0022-2836(03)00596-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report