4R53
dihydrodipicolinate synthase from C. jejuni with vacant active site and vacant allosteric site
Summary for 4R53
Entry DOI | 10.2210/pdb4r53/pdb |
Related | 4LY8 4M19 4MLJ 4MLR |
Descriptor | 4-hydroxy-tetrahydrodipicolinate synthase, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (7 entities in total) |
Functional Keywords | schiff-base, aldolase, tim barrel, lyase |
Biological source | Campylobacter jejuni subsp. jejuni |
Cellular location | Cytoplasm : Q9PPB4 |
Total number of polymer chains | 4 |
Total formula weight | 136223.39 |
Authors | Conly, C.J.T. (deposition date: 2014-08-20, release date: 2015-10-07, Last modification date: 2024-02-28) |
Primary citation | Conly, C.J.,Skovpen, Y.V.,Li, S.,Palmer, D.R.,Sanders, D.A. Tyrosine 110 plays a critical role in regulating the allosteric inhibition of Campylobacter jejuni dihydrodipicolinate synthase by lysine. Biochemistry, 53:7396-7406, 2014 Cited by PubMed: 25369463DOI: 10.1021/bi5012157 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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