1E19

Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP

Summary for 1E19

Related1B7B
DescriptorCARBAMATE KINASE, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordstransferase, hyperthermophiles, adp site, arginine metabolism phosphoryl group transfer
Biological sourcePYROCOCCUS FURIOSUS
Cellular locationCytoplasm P95474
Total number of polymer chains2
Total molecular weight69854.18
Authors
Ramon-Maiques, S.,Marina, A.,Uriarte, M.,Fita, I.,Rubio, V. (deposition date: 2000-04-28, release date: 2000-07-04, Last modification date: 2012-05-30)
Primary citation
Ramon-Maiques, S.,Marina, A.,Uriarte, M.,Fita, I.,Rubio, V.
The 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase from the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms that This Thermoestable Enzyme is a Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases
J.Mol.Biol., 299:463-, 2000
PubMed: 10860751 (PDB entries with the same primary citation)
DOI: 10.1006/JMBI.2000.3779
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.5 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.20890.2%2.2%5.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution