1COM
THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS: STRUCTURE DETERMINATION OF CHORISMATE MUTASE AND ITS COMPLEXES WITH A TRANSITION STATE ANALOG AND PREPHENATE, AND IMPLICATIONS ON THE MECHANISM OF ENZYMATIC REACTION
Summary for 1COM
Entry DOI | 10.2210/pdb1com/pdb |
Descriptor | CHORISMATE MUTASE, PREPHENIC ACID (3 entities in total) |
Functional Keywords | chorismate mutase |
Biological source | Bacillus subtilis |
Cellular location | Cytoplasm : P19080 |
Total number of polymer chains | 12 |
Total formula weight | 176130.63 |
Authors | Chook, Y.M.,Ke, H.,Lipscomb, W.N. (deposition date: 1994-04-08, release date: 1994-06-22, Last modification date: 2024-02-07) |
Primary citation | Chook, Y.M.,Gray, J.V.,Ke, H.,Lipscomb, W.N. The monofunctional chorismate mutase from Bacillus subtilis. Structure determination of chorismate mutase and its complexes with a transition state analog and prephenate, and implications for the mechanism of the enzymatic reaction. J.Mol.Biol., 240:476-500, 1994 Cited by PubMed: 8046752DOI: 10.1006/jmbi.1994.1462 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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