5D6B
Human fumarase (wild type)
Summary for 5D6B
| Entry DOI | 10.2210/pdb5d6b/pdb |
| Descriptor | Fumarate hydratase, mitochondrial (2 entities in total) |
| Functional Keywords | lyase, tca cycle, fumarate hydratase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 49739.01 |
| Authors | Pereira de Padua, R.A.,Nonato, M.C. (deposition date: 2015-08-11, release date: 2016-08-24, Last modification date: 2024-03-06) |
| Primary citation | Pereira de Padua, R.A.,Nonato, M.C. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase. Acta Crystallogr F Struct Biol Commun, 70:120-122, 2014 Cited by PubMed Abstract: Human fumarase (HsFH) is a well-known citric acid cycle enzyme and is therefore a key component in energy metabolism. Genetic studies on human patients have shown that polymorphisms in the fumarase gene are responsible for diseases such as hereditary leiomyomatosis and renal cell cancer. As a first step in unravelling the molecular basis of the mechanism of fumarase deficiency in genetic disorders, the HsFH gene was cloned in pET-28a, heterologously expressed in Escherichia coli, purified by nickel-affinity chromatography and crystallized using the vapour-diffusion technique. X-ray diffraction experiments were performed at a synchrotron source and the structure was solved at 2.1 Å resolution by molecular replacement. PubMed: 24419633DOI: 10.1107/S2053230X13033955 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
