2GVN
L-asparaginase from Erwinia carotovora in complex with aspartic acid
Summary for 2GVN
| Entry DOI | 10.2210/pdb2gvn/pdb |
| Related | 1ZCF |
| Descriptor | L-asparaginase, ASPARTIC ACID (3 entities in total) |
| Functional Keywords | l-asparaginase, erwinia carotovora, hydrolase |
| Biological source | Pectobacterium atrosepticum |
| Total number of polymer chains | 8 |
| Total formula weight | 277290.95 |
| Authors | Kravchenko, O.V.,Kislitsin, Y.A.,Popov, A.N.,Nikonov, S.V.,Kuranova, I.P. (deposition date: 2006-05-03, release date: 2007-05-15, Last modification date: 2023-08-30) |
| Primary citation | Kravchenko, O.V.,Kislitsin, Y.A.,Popov, A.N.,Nikonov, S.V.,Kuranova, I.P. Three-dimensional structures of L-asparaginase from Erwinia carotovora complexed with aspartate and glutamate. Acta Crystallogr.,Sect.D, 64:248-256, 2008 Cited by PubMed Abstract: The crystal structures of Erwinia carotovora L-asparaginase complexed with L-aspartate and L-glutamate were determined at 1.9 and 2.2 A, respectively, using the molecular-replacement method and were refined to R factors of about 21% in both cases. The positions of the ligands in the active site were located. A comparison of the new structures with the known structures of Escherichia coli L-asparaginase and Er. chrysanthemi L-asparaginase was performed. It was found that the arrangement of the ligands practically coincides in all three enzymes. The peculiarities of the quaternary structure of the enzyme, the possible role of water molecules in the enzyme action and the conformational changes during the catalyzed reaction are discussed. PubMed: 18323619DOI: 10.1107/S0907444907065766 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
