2WNQ

Structure of the E192N mutant of E. coli N-acetylneuraminic acid lyase in space group P21

Summary for 2WNQ

Entry DOI	10.2210/pdb2wnq/pdb
Related	1FDY 1FDZ 1HL2 1NAL 2WKJ 2WNN 2WNZ 2WO5 2WPB 2WSG
Descriptor	N-ACETYLNEURAMINATE LYASE, CHLORIDE ION (3 entities in total)
Functional Keywords	substrate specificity, carbohydrate metabolism, directed evolution, protein engineering, lyase, aldolase
Biological source	ESCHERICHIA COLI
Cellular location	Cytoplasm: P0A6L4
Total number of polymer chains	4
Total formula weight	134419.23
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: 2009-07-17, release date: 2010-08-25, Last modification date: 2023-12-13)
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: 20826162 DOI: 10.1016/J.JMB.2010.08.008 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation