4ECA
ASPARAGINASE FROM E. COLI, MUTANT T89V WITH COVALENTLY BOUND ASPARTATE
Summary for 4ECA
Entry DOI | 10.2210/pdb4eca/pdb |
Descriptor | L-ASPARAGINE AMIDOHYDROLASE (2 entities in total) |
Functional Keywords | hydrolase, acyl-enzyme intermediate, threonine amidohydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 138959.70 |
Authors | Palm, G.J.,Lubkowski, J.,Wlodawer, A. (deposition date: 1997-02-21, release date: 1997-06-16, Last modification date: 2023-08-09) |
Primary citation | Palm, G.J.,Lubkowski, J.,Derst, C.,Schleper, S.,Rohm, K.H.,Wlodawer, A. A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant. FEBS Lett., 390:211-216, 1996 Cited by PubMed: 8706862DOI: 10.1016/0014-5793(96)00660-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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