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1B7B
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CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS
Descriptor:CARBAMATE KINASE, SULFATE ION
Authors:Marina, A., Alzari, P.M., Bravo, J., Uriarte, M., Barcelona, B., Fita, I., Rubio, V.
Deposit date:1999-01-20
Release date:2000-01-26
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.
Protein Sci., 8, 1999
1E19
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STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS BOUND TO ADP
Descriptor:CARBAMATE KINASE, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION
Authors:Ramon-Maiques, S., Marina, A., Uriarte, M., Fita, I., Rubio, V.
Deposit date:2000-04-28
Release date:2000-07-04
Last modified:2012-05-30
Method:X-RAY DIFFRACTION (1.5 Å)
Cite: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, 2000
2WE4
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CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO A SULFATE ION AND TWO WATER MOLECULES, WHICH MIMIC THE SUBSTRATE CARBAMYL PHOSPHATE
Descriptor:CARBAMATE KINASE 1, SULFATE ION
Authors:Ramon-Maiques, S., Marina, A., Gil-Ortiz, F., Rubio, V.
Deposit date:2009-03-27
Release date:2010-03-16
Last modified:2019-05-08
Method:X-RAY DIFFRACTION (2.02 Å)
Cite: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, 2010
2WE5
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CARBAMATE KINASE FROM ENTEROCOCCUS FAECALIS BOUND TO MGADP
Descriptor:CARBAMATE KINASE 1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ...
Authors:Ramon-Maiques, S., Marina, A., Rubio, V.
Deposit date:2009-03-27
Release date:2010-03-16
Last modified:2019-05-08
Method:X-RAY DIFFRACTION (1.39 Å)
Cite: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, 2010