5EUN
The Crystal Structure of Human Kynurenine Aminotransferase II, PLP-bound form, at 1.83 A
Summary for 5EUN
| Entry DOI | 10.2210/pdb5eun/pdb |
| Descriptor | Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (2 entities in total) |
| Functional Keywords | kynurenine aminotransferase ii, llp, transferase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Mitochondrion : Q8N5Z0 |
| Total number of polymer chains | 1 |
| Total formula weight | 47628.55 |
| Authors | Nematollahi, A.,Sun, G.,Kwan, A.,Jeffries, C.M.,Harrop, S.J.,Hanrahan, J.R.,Nadvi, N.A.,Church, W.B. (deposition date: 2015-11-18, release date: 2015-12-16, Last modification date: 2016-08-10) |
| Primary citation | Nematollahi, A.,Sun, G.,Harrop, S.J.,Hanrahan, J.R.,Church, W.B. Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 angstrom Resolution. Int J Mol Sci, 17:446-446, 2016 Cited by PubMed Abstract: Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia. In order to fully describe the role of KAT-II in the pathobiology of schizophrenia and other brain disorders, the crystal structure of full-length PLP-form hKAT-II was determined at 1.83 Å resolution, the highest available. The electron density of the active site reveals an aldimine linkage between PLP and Lys263, as well as the active site residues, which characterize the fold-type I PLP-dependent enzymes. PubMed: 27023527DOI: 10.3390/ijms17040446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.825 Å) |
Structure validation
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