5TIC
X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5
Summary for 5TIC
Entry DOI | 10.2210/pdb5tic/pdb |
Related | 5TID 5TIE 5TIF |
Descriptor | Acyl-CoA thioesterase I, CHLORIDE ION (3 entities in total) |
Functional Keywords | thioesterase, tesa, fatty acid, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 41478.52 |
Authors | Thoden, J.B.,Holden, H.M.,Grisewood, M.J.,Hernandez Lozada, N.J.,Gifford, N.P.,Mendez-Perez, D.,Schoenberger, H.A.,Allan, M.F.,Pfleger, B.F.,Marines, C.D. (deposition date: 2016-10-02, release date: 2017-04-26, Last modification date: 2023-10-04) |
Primary citation | Grisewood, M.J.,Hernandez Lozada, N.J.,Thoden, J.B.,Gifford, N.P.,Mendez-Perez, D.,Schoenberger, H.A.,Allan, M.F.,Floy, M.E.,Lai, R.Y.,Holden, H.M.,Pfleger, B.F.,Maranas, C.D. Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids. ACS Catal, 7:3837-3849, 2017 Cited by PubMed: 29375928DOI: 10.1021/acscatal.7b00408 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report