1e19
From Proteopedia
(Difference between revisions)
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| - | {{Seed}} | ||
[[Image:1e19.png|left|200px]] | [[Image:1e19.png|left|200px]] | ||
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{{STRUCTURE_1e19| PDB=1e19 | SCENE= }} | {{STRUCTURE_1e19| PDB=1e19 | SCENE= }} | ||
| - | === | + | ===Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP=== |
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1e19]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E19 OCA]. | |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:010860751</ref><references group="xtra"/> |
[[Category: Carbamate kinase]] | [[Category: Carbamate kinase]] | ||
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
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[[Category: Uriarte, M.]] | [[Category: Uriarte, M.]] | ||
[[Category: Adp site]] | [[Category: Adp site]] | ||
| - | [[Category: Arginine metabolism]] | + | [[Category: Arginine metabolism phosphoryl group transfer]] |
[[Category: Hyperthermophile]] | [[Category: Hyperthermophile]] | ||
| - | [[Category: | + | [[Category: Transferase]] |
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Revision as of 05:04, 30 May 2012
Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP
Template:ABSTRACT PUBMED 10860751
About this Structure
1e19 is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
- 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 thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol. 2000 Jun 2;299(2):463-76. PMID:10860751 doi:http://dx.doi.org/10.1006/jmbi.2000.3779
