1E19
Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP
Summary for 1E19
Entry DOI | 10.2210/pdb1e19/pdb |
Related | 1B7B |
Descriptor | CARBAMATE KINASE, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | transferase, hyperthermophiles, adp site, arginine metabolism phosphoryl group transfer |
Biological source | PYROCOCCUS FURIOSUS |
Cellular location | Cytoplasm: P95474 |
Total number of polymer chains | 2 |
Total formula weight | 69854.18 |
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 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 Cited by PubMed: 10860751DOI: 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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