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[2bty] replaced from '1uvv'

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<Asymmetric unit>

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PDB ID2bty  sequence information (FASTA format)   
DescriptorACETYLGLUTAMATE KINASE (E.C.2.7.2.8)
TitleACETYLGLUTAMATE KINASE FROM THERMOTOGA MARITIMA COMPLEXED WITH ITS INHIBITOR ARGININE
Functional KeywordsN-ACETYL-L-GLUTAMATE KINASE, AMINO ACID KINASE, PHOSPHORYL GROUP TRANSFER, ARGININE METABOLISM, TRANSFERASE, ARGININE BIOSYNTHESIS, AMINO-ACID BIOSYNTHESIS, KINASE
Biological sourceTHERMOTOGA MARITIMA
Cellular location [UNP - Q9X2A4] Cytoplasm (Probable)
Total number of polymer chains3
Total molecular weight92289.7 (the details in Structural Details Page)
AuthorsGil-Ortiz, F. , Fernandez-Murga, M.L. , Fita, I. , Rubio, V. (deposition date : 2005-06-08, release date : 2005-12-13)
Primary citationRamon-Maiques, S. , Fernandez-Murga, M.L. , Gil-Ortiz, F. , Vagin, A. , Fita, I. , Rubio, V.
Structural Bases of Feed-Back Control of Arginine Biosynthesis, Revealed by the Structure of Two Hexameric N-Acetylglutamate Kinases, from Thermotoga Maritima and Pseudomonas Aeruginosa
J.Mol.Biol., 356:695 - , 2006.(PubMed : 16376937)  (DOI: 10.1016/J.JMB.2005.11.079)
Experimental methodX-RAY DIFFRACTION ( 2.75[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( Q9X2A4 ) , eF-site , KEGG ( EC 2.7.2.8 ) , PISA