1LM4

Structure of Peptide Deformylase from Staphylococcus aureus at 1.45 A

Summary for 1LM4

Related1LM6 1LME
Descriptorpeptide deformylase PDF1, FE (III) ION, GLYCEROL, ... (4 entities in total)
Functional Keywordspdf, metalloenzyme, staphylococcus aureus, hydrolase
Biological sourceStaphylococcus aureus
Total number of polymer chains2
Total molecular weight44137.8
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: 2014-11-12)
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
PubMed: 12823970 (PDB entries with the same primary citation)
DOI: 10.1016/S0022-2836(03)00596-5
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.45 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers800.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution