4JAE
STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI complexed WITH S-CARBOXYMETHYL-COA
Replaces: 3L97Summary for 4JAE
Entry DOI | 10.2210/pdb4jae/pdb |
Related | 4G6B 4JAD 4JAF 4JAG |
Descriptor | Citrate synthase, SULFATE ION, CARBOXYMETHYL COENZYME *A, ... (4 entities in total) |
Functional Keywords | citrate synthase, gram-negative bacteria, allostery, oxaloacetate, acetyl-coa, nadh, protein folding, s-carboxymethyl-coa, allosteric enzyme, transferase, tricarboxylic acid cycle |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 98024.96 |
Authors | Maurus, R.,Brayer, G.D. (deposition date: 2013-02-18, release date: 2013-07-17, Last modification date: 2023-09-20) |
Primary citation | Duckworth, H.W.,Nguyen, N.T.,Gao, Y.,Donald, L.J.,Maurus, R.,Ayed, A.,Bruneau, B.,Brayer, G.D. Enzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding. Biochim.Biophys.Acta, 1834:2546-2553, 2013 Cited by PubMed: 23954305DOI: 10.1016/j.bbapap.2013.07.019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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