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1E19

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

Summary for 1E19
Entry DOI10.2210/pdb1e19/pdb
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 formula 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: 2023-12-06)
Primary citationRamon-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
Cited by
PubMed: 10860751
DOI: 10.1006/JMBI.2000.3779
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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