2V30

Human orotidine 5'-phosphate decarboxylase domain of uridine monophospate synthetase (UMPS) in complex with its product UMP.

Summary for 2V30

Related2JGY
DescriptorOROTIDINE 5'-PHOSPHATE DECARBOXYLASE, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
Functional Keywordsalternative splicing, pyrimidine metabolism, disease mutation, glycosyltransferase, ump, lyase, transferase, polymorphism, decarboxylase, multifunctional enzyme, pyrimidine biosynthesis
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains2
Total molecular weight61910.83
Authors
Primary citation
Moche, M.,Ogg, D.,Arrowsmith, C.,Berglund, H.,Busam, R.,Collins, R.,Dahlgren, L.G.,Edwards, A.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Hallberg, B.M.,Holmberg-Schiavone, L.,Johansson, I.,Kallas, A.,Karlberg, T.,Kotenyova, T.,Lehtio, L.,Nyman, T.,Persson, C.,Sagemark, J.,Stenmark, P.,Sundstrom, M.,Thorsell, A.G.,van den Berg, S.,Weigelt, J.,Welin, M.,Nordlund, P.
The Crystal Structure of Human Orotidine 5'-Decarboxylase Domain of Human Uridine Monophosphate Synthetase (Umps)
To be Published,
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.195500.7%2.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution