5HEE
Crystal structure of the TK2203 protein
Summary for 5HEE
| Entry DOI | 10.2210/pdb5hee/pdb |
| Descriptor | Putative uncharacterized protein, TK2203 protein, ZINC ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | putative, dioxygenase, oxidoreductase |
| Biological source | Thermococcus kodakarensis KOD1 |
| Total number of polymer chains | 2 |
| Total formula weight | 59374.63 |
| Authors | Nishitani, Y.,Miki, K. (deposition date: 2016-01-06, release date: 2016-06-29, Last modification date: 2024-03-20) |
| Primary citation | Nishitani, Y.,Simons, J.R.,Kanai, T.,Atomi, H.,Miki, K. Crystal structure of the TK2203 protein from Thermococcus kodakarensis, a putative extradiol dioxygenase Acta Crystallogr.,Sect.F, 72:427-433, 2016 Cited by PubMed Abstract: The TK2203 protein from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (262 residues, 29 kDa) is a putative extradiol dioxygenase catalyzing the cleavage of C-C bonds in catechol derivatives. It contains three metal-binding residues, but has no significant sequence similarity to proteins for which structures have been determined. Here, the first crystal structure of the TK2203 protein was determined at 1.41 Å resolution to investigate its functional role. Structure analysis reveals that this protein shares the same fold and catalytic residues as other extradiol dioxygenases, strongly suggesting the same enzymatic activity. Furthermore, the important region contributing to substrate selectivity is discussed. PubMed: 27303894DOI: 10.1107/S2053230X16006920 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.41 Å) |
Structure validation
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