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5TIC

X-ray structure of wild-type E. coli Acyl-CoA thioesterase I at pH 5

Summary for 5TIC
Entry DOI10.2210/pdb5tic/pdb
Related5TID 5TIE 5TIF
DescriptorAcyl-CoA thioesterase I, CHLORIDE ION (3 entities in total)
Functional Keywordsthioesterase, tesa, fatty acid, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight41478.52
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 citationGrisewood, 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: 29375928
DOI: 10.1021/acscatal.7b00408
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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