6PAC
E. coli L-asparaginase II in complex with L-Asp at pH 5.6
Summary for 6PAC
| Entry DOI | 10.2210/pdb6pac/pdb |
| Descriptor | L-asparaginase 2, ASPARTIC ACID, IMIDAZOLE, ... (4 entities in total) |
| Functional Keywords | inactive mutant, hydrolysis of l-asparagine, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 4 |
| Total formula weight | 143478.44 |
| Authors | Lubkowski, J.,Wlodawer, A. (deposition date: 2019-06-11, release date: 2019-09-04, Last modification date: 2024-11-13) |
| Primary citation | Lubkowski, J.,Wlodawer, A. Geometric considerations support the double-displacement catalytic mechanism of l-asparaginase. Protein Sci., 28:1850-1864, 2019 Cited by PubMed Abstract: Twenty crystal structures of the complexes of l-asparaginase with l-Asn, l-Asp, and succinic acid that are currently available in the Protein Data Bank, as well as 11 additional structures determined in the course of this project, were analyzed in order to establish the level of conservation of the geometric parameters describing interactions between the substrates and the active site of the enzymes. We found that such stereochemical relationships are highly conserved, regardless of the organism from which the enzyme was isolated, specific crystallization conditions, or the nature of the ligands. Analysis of the geometry of the interactions, including Bürgi-Dunitz and Flippin-Lodge angles, indicated that Thr12 (Escherichia coli asparaginase II numbering) is optimally placed to be the primary nucleophile in the most likely scenario utilizing a double-displacement mechanism, whereas catalysis through a single-displacement mechanism appears to be the least likely. PubMed: 31423681DOI: 10.1002/pro.3709 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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