7QY6
Structure of E.coli Class 2 L-asparaginase EcAIII, wild type (WT EcAIII)
This is a non-PDB format compatible entry.
Summary for 7QY6
Entry DOI | 10.2210/pdb7qy6/pdb |
Related | 7QQ8 7QSF 7QTC 7QVR |
Descriptor | Isoaspartyl peptidase, Beta-aspartyl-peptidase, SODIUM ION, ... (5 entities in total) |
Functional Keywords | l-asparaginase, mutation, hydrolase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 67000.72 |
Authors | Loch, J.I.,Klonecka, A.,Kadziolka, K.,Bonarek, P.,Barciszewski, J.,Imiolczyk, B.,Brzezinski, K.,Jaskolski, M. (deposition date: 2022-01-27, release date: 2022-07-13, Last modification date: 2024-01-31) |
Primary citation | Loch, J.I.,Klonecka, A.,Kadziolka, K.,Bonarek, P.,Barciszewski, J.,Imiolczyk, B.,Brzezinski, K.,Gilski, M.,Jaskolski, M. Structural and biophysical studies of new L-asparaginase variants: lessons from random mutagenesis of the prototypic Escherichia coli Ntn-amidohydrolase. Acta Crystallogr D Struct Biol, 78:911-926, 2022 Cited by PubMed: 35775990DOI: 10.1107/S2059798322005691 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report