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6EOK

Crystal structure of E. coli L-asparaginase II

Summary for 6EOK
Entry DOI10.2210/pdb6eok/pdb
Related1IHD 1JAZ 1NNS 3ECA
DescriptorL-asparaginase 2, ZINC ION (3 entities in total)
Functional Keywordsl-asparaginase ii, hydrolase
Biological sourceEscherichia coli (strain K12)
Total number of polymer chains4
Total formula weight138768.87
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 citationCerofolini, 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: 30462348
DOI: 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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