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PDBe Entry: 1ohb view

ACETYLGLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ADP AND SULPHATE
Summary
Header KINASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.9 Å, R-factor: 19.48%, Free R-factor: 22.11%, Spacegroup: C 2 2 21
Released 31/07/2003, deposition: 23/05/2003, last revision: 24/02/2009
Authors Gil-Ortiz, F.search; Ramon-Maiques, S.search; Fita, I.search; Rubio, V.search
Primary citation The Course of Phosphorus in the Reaction of N-Acetyl-L-Glutamate Kinase, Determined from the Structures of Crystalline Complexes, Including a Complex with an Alf(4)(-) Transition State Mimic
J.MOL.BIOL.search vol:331, pag:231 (2003) [PubMed ID 12875848 ]search
Keywords KINASEsearch, N-ACETYL-L-GLUTAMATE KINASEsearch, AMINO ACID KINASEsearch, PHOSPHORYL GROUP TRANSFERsearch, ARGININE METABOLISMsearch, X-RAY DIFFRACTIONsearch
EC 2.7.2.8 ExPASy BRENDA search (A)
Organism Escherichia coli 562search(A)
UniProt Acetylglutamate kinase (EC 2.7.2.8) (NAG kinase) (AGK) (N-acetyl-L-glutamate 5-phosphotransferase) P0A6C8search (A)
Solvent A
Related entries 1gs5, 1gsj, 1oh9, 1oha
Polymers
Id Name Type UniProt Residues Observed
A ACETYLGLUTAMATE KINASE Protein P0A6C8 (ARGB_ECOLI)search
258 100%
Heterogens
Id Name Ligands
A SULFATE ION SO4 search
A ADENOSINE-5'-DIPHOSPHATE ADP search
A ACETATE ION ACT search
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