6SLL
Diaminobutyrate acetyltransferase EctA from Paenibacillus lautus in complex with its substrate L-2,4-diaminobutyric acid (DAB) and coenzyme A
Summary for 6SLL
Entry DOI | 10.2210/pdb6sll/pdb |
Descriptor | L-2,4-diaminobutyric acid acetyltransferase, COENZYME A, 2,4-DIAMINOBUTYRIC ACID, ... (5 entities in total) |
Functional Keywords | l-2, 4-diaminobutyrate acetyltransferase, acetyl coenzyme a, acetylation, stress response, chemical chaperone, transferase |
Biological source | Geobacillus sp. (strain Y412MC10) |
Total number of polymer chains | 2 |
Total formula weight | 43450.44 |
Authors | Richter, A.A.,Kobus, S.,Czech, L.,Hoeppner, A.,Bremer, E.,Smits, S.H.J. (deposition date: 2019-08-20, release date: 2020-01-29, Last modification date: 2024-01-24) |
Primary citation | Richter, A.A.,Kobus, S.,Czech, L.,Hoeppner, A.,Zarzycki, J.,Erb, T.J.,Lauterbach, L.,Dickschat, J.S.,Bremer, E.,Smits, S.H.J. The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine. J.Biol.Chem., 295:2822-2838, 2020 Cited by PubMed: 31969391DOI: 10.1074/jbc.RA119.011277 PDB entries with the same primary citation |
Experimental method |
Structure validation
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