6SBI
X-ray structure of murine Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate
Summary for 6SBI
| Entry DOI | 10.2210/pdb6sbi/pdb |
| Descriptor | Acylpyruvase FAHD1, mitochondrial, MAGNESIUM ION, POTASSIUM ION, ... (6 entities in total) |
| Functional Keywords | oxalate binding, tca cycle, mitochondria, hydrolase |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 4 |
| Total formula weight | 118498.54 |
| Authors | Rupp, B.,Naschberger, A.,Weiss, A.K.H. (deposition date: 2019-07-21, release date: 2020-03-25, Last modification date: 2024-01-24) |
| Primary citation | Weiss, A.K.H.,Naschberger, A.,Cappuccio, E.,Metzger, C.,Mottes, L.,Holzknecht, M.,von Velsen, J.,Bowler, M.W.,Rupp, B.,Jansen-Durr, P. Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse. Biosci.Rep., 40:-, 2020 Cited by PubMed Abstract: FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1. PubMed: 32068790DOI: 10.1042/BSR20194431 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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