2WO5
Structure of wild type E. coli N-acetylneuraminic acid lyase in space group P21 crystal form I
Summary for 2WO5
Entry DOI | 10.2210/pdb2wo5/pdb |
Related | 1FDY 1FDZ 1HL2 1NAL 2WKJ 2WNN 2WNQ 2WNZ 2WPB 2WSG |
Descriptor | N-ACETYLNEURAMINATE LYASE (2 entities in total) |
Functional Keywords | substrate specificity, carbohydrate metabolism, directed evolution, protein engineering, lyase, aldolase, schiff base |
Biological source | ESCHERICHIA COLI |
Cellular location | Cytoplasm: P0A6L4 |
Total number of polymer chains | 4 |
Total formula weight | 134337.47 |
Authors | Campeotto, I.,Bolt, A.H.,Harman, T.A.,Trinh, C.H.,Dennis, C.A.,Phillips, S.E.V.,Pearson, A.R.,Nelson, A.,Berry, A. (deposition date: 2009-07-21, release date: 2010-08-25, Last modification date: 2023-12-20) |
Primary citation | Campeotto, I.,Bolt, A.H.,Harman, T.A.,Dennis, C.A.,Trinh, C.H.,Phillips, S.E.V.,Nelson, A.,Pearson, A.R.,Berry, A. Structural Insights Into Substrate Specificity in Variants of N-Acetylneuraminic Acid Lyase Produced by Directed Evolution. J.Mol.Biol., 404:56-, 2010 Cited by PubMed: 20826162DOI: 10.1016/J.JMB.2010.08.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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