4AMA
Crystal Structure of N-acetylneuraminic acid lyase from Staphylococcus aureus with the chemical modification thia-lysine at position 165 in complex with pyruvate
Summary for 4AMA
Entry DOI | 10.2210/pdb4ama/pdb |
Related | 4AH7 4AHO 4AHP 4AHQ |
Descriptor | N-ACETYLNEURAMINATE LYASE (2 entities in total) |
Functional Keywords | lyase, conversion on pyruvate and d-acetyl mannosamine to n-acetylneuraminic acid |
Biological source | STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325 |
Total number of polymer chains | 4 |
Total formula weight | 135444.89 |
Authors | Timms, N.,Polyakova, A.,Windle, C.L.,Trinh, C.H.,Nelson, A.,Pearson, A.R.,Berry, A. (deposition date: 2012-03-08, release date: 2013-01-23, Last modification date: 2019-07-10) |
Primary citation | Timms, N.,Windle, C.L.,Polyakova, A.,Ault, J.R.,Trinh, C.H.,Pearson, A.R.,Nelson, A.,Berry, A. Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with gamma-thialysine by using a chemical mutagenesis strategy. Chembiochem, 14:474-481, 2013 Cited by PubMed: 23418011DOI: 10.1002/cbic.201200714 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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