Summary for 5SYH
| Entry DOI | 10.2210/pdb5syh/pdb |
| Related | 5L02 5L05 5SW4 5SW5 5SW6 5SX0 5SX1 5SX2 5SX3 5SX6 5SX7 5SXQ 5SXR 5SXS 5SXT 5SXX 5SYI 5SYJ 5SYK 5SYL 5SYU 5SYV 5SYW 5SYX 5SYY |
| Descriptor | Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (8 entities in total) |
| Functional Keywords | catalase-peroxidase, katg, d141a variant, oxidoreductase |
| Biological source | Burkholderia pseudomallei (strain 1710b) |
| Total number of polymer chains | 2 |
| Total formula weight | 161126.45 |
| Authors | Loewen, P.C. (deposition date: 2016-08-11, release date: 2016-09-07, Last modification date: 2023-11-15) |
| Primary citation | Loewen, P.C.,Carpena, X.,Vidossich, P.,Fita, I.,Rovira, C. An ionizable active-site tryptophan imparts catalase activity to a peroxidase core. J. Am. Chem. Soc., 136:7249-7252, 2014 Cited by PubMed Abstract: Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatG's involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp. PubMed: 24785434DOI: 10.1021/ja502794e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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