2WE5

Carbamate kinase from Enterococcus faecalis bound to MgADP

Summary for 2WE5

DescriptorCARBAMATE KINASE 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsarginine catabolism, arginine metabolism, atp synthesys, kinase, open alpha/beta sheet, phosphotransferase, transferase
Biological sourceENTEROCOCCUS FAECALIS
Total number of polymer chains3
Total molecular weight100289.3
Authors
Ramon-Maiques, S.,Marina, A.,Rubio, V. (deposition date: 2009-03-27, release date: 2010-03-16, Last modification date: 2019-07-24)
Primary citation
Ramon-Maiques, S.,Marina, A.,Guinot, A.,Gil-Ortiz, F.,Uriarte, M.,Fita, I.,Rubio, V.
Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site- Directed Mutagenesis Studies. Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria.
J.Mol.Biol., 397:1261-, 2010
PubMed: 20188742 (PDB entries with the same primary citation)
DOI: 10.1016/J.JMB.2010.02.038
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.39 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.2167 0.2% 1.2% 10.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution