7AYC
Crystal Structure of human mitochondrial 2-Enoyl Thioester Reductase (MECR) with single mutation G165Q
Summary for 7AYC
Entry DOI | 10.2210/pdb7ayc/pdb |
Related | 7AYB 7AYD |
Descriptor | Enoyl-[acyl-carrier-protein] reductase, mitochondrial, CHLORIDE ION (3 entities in total) |
Functional Keywords | medium-chain alcohol dehydrogenase, mitochondrial trans-2-enoyl-coa reductase, fatty acid synthesis, oxidoreductase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 38470.43 |
Authors | Rahman, M.T.,Koski, M.K.,Autio, K.J.,Kastaniotis, A.J.,Wierenga, R.K.,Hiltunen, J.K. (deposition date: 2020-11-12, release date: 2022-06-01, Last modification date: 2024-02-07) |
Primary citation | Tanvir Rahman, M.,Kristian Koski, M.,Panecka-Hofman, J.,Schmitz, W.,Kastaniotis, A.J.,Wade, R.C.,Wierenga, R.K.,Kalervo Hiltunen, J.,Autio, K.J. An engineered variant of MECR reductase reveals indispensability of long-chain acyl-ACPs for mitochondrial respiration. Nat Commun, 14:619-619, 2023 Cited by PubMed: 36739436DOI: 10.1038/s41467-023-36358-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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