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2WO5

Structure of wild type E. coli N-acetylneuraminic acid lyase in space group P21 crystal form I

Summary for 2WO5
Entry DOI10.2210/pdb2wo5/pdb
Related1FDY 1FDZ 1HL2 1NAL 2WKJ 2WNN 2WNQ 2WNZ 2WPB 2WSG
DescriptorN-ACETYLNEURAMINATE LYASE (2 entities in total)
Functional Keywordssubstrate specificity, carbohydrate metabolism, directed evolution, protein engineering, lyase, aldolase, schiff base
Biological sourceESCHERICHIA COLI
Cellular locationCytoplasm: P0A6L4
Total number of polymer chains4
Total formula weight134337.47
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 citationCampeotto, 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 (2.2 Å)
Structure validation

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