5DJ3

Structure of the PLP-Dependent L-Arginine Hydroxylase MppP with D-Arginine Bound

Summary for 5DJ3

Related5DJ1
DescriptorPLP-Dependent L-Arginine Hydroxylase MppP, (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsaminotransferase, hydroxylase, enduracididine, pyridoxal 5'-phosphate, transferase
Biological sourceStreptomyces wadayamensis
Total number of polymer chains4
Total molecular weight167788.62
Authors
Silvaggi, N.R.,Han, L. (deposition date: 2015-09-01, release date: 2015-11-25, Last modification date: 2015-12-16)
Primary citation
Han, L.,Schwabacher, A.W.,Moran, G.R.,Silvaggi, N.R.
Streptomyces wadayamensis MppP Is a Pyridoxal 5'-Phosphate-Dependent l-Arginine alpha-Deaminase, gamma-Hydroxylase in the Enduracididine Biosynthetic Pathway.
Biochemistry, 54:7029-7040, 2015
PubMed: 26551990 (PDB entries with the same primary citation)
DOI: 10.1021/acs.biochem.5b01016
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.227 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.204500.6%2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution