1F14
L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)
Summary for 1F14
| Entry DOI | 10.2210/pdb1f14/pdb |
| Related | 1F0Y 1F12 1F17 3HAD |
| Descriptor | L-3-HYDROXYACYL-COA DEHYDROGENASE (2 entities in total) |
| Functional Keywords | l-3-hydroxyacyl-coa (apoenzyme), oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion matrix: Q16836 |
| Total number of polymer chains | 2 |
| Total formula weight | 67791.65 |
| Authors | Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J. (deposition date: 2000-05-18, release date: 2000-09-27, Last modification date: 2024-02-07) |
| Primary citation | Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.,Banaszak, L.J. Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J.Biol.Chem., 275:27186-27196, 2000 Cited by PubMed: 10840044PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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