1HL2
Crystal structure of N-acetylneuraminate lyase from E. coli mutant L142R in complex with b-hydroxypyruvate
Summary for 1HL2
Entry DOI | 10.2210/pdb1hl2/pdb |
Related | 1FDY 1FDZ 1NAL |
Descriptor | N-ACETYLNEURAMINATE LYASE SUBUNIT, 3-HYDROXYPYRUVIC ACID (3 entities in total) |
Functional Keywords | n-acetylneuraminate lyase, class i aldolase, lyase, carbohydrate metabolism, schiff base |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 4 |
Total formula weight | 131097.88 |
Authors | Joerger, A.C.,Fersht, A.R. (deposition date: 2003-03-12, release date: 2003-05-09, Last modification date: 2023-12-13) |
Primary citation | Joerger, A.C.,Mayer, S.,Fersht, A.R. Mimicking Natural Evolution in Vitro: An N-Acetylneuraminate Lyase Mutant with an Increased Dihydrodipicolinate Synthase Activity Proc.Natl.Acad.Sci.USA, 100:5694-, 2003 Cited by PubMed: 12711733DOI: 10.1073/PNAS.0531477100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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