6EOK
Crystal structure of E. coli L-asparaginase II
Summary for 6EOK
| Entry DOI | 10.2210/pdb6eok/pdb |
| Related | 1IHD 1JAZ 1NNS 3ECA |
| Descriptor | L-asparaginase 2, ZINC ION (3 entities in total) |
| Functional Keywords | l-asparaginase ii, hydrolase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 4 |
| Total formula weight | 138768.87 |
| Authors | Cerofolini, L.,Giuntini, S.,Carlon, A.,Ravera, E.,Calderone, V.,Fragai, M.,Parigi, G.,Luchinat, C. (deposition date: 2017-10-09, release date: 2018-10-31, Last modification date: 2024-11-06) |
| Primary citation | Cerofolini, L.,Giuntini, S.,Carlon, A.,Ravera, E.,Calderone, V.,Fragai, M.,Parigi, G.,Luchinat, C. Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics. Chemistry, 25:1984-1991, 2019 Cited by PubMed Abstract: Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography. PubMed: 30462348DOI: 10.1002/chem.201804488 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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