3WHN

Hemerythrin-like domain of DcrH I119H mutant (met)

Summary for 3WHN

Entry DOI	10.2210/pdb3whn/pdb
Related	3AGT 3AGU 3WAQ
Descriptor	Hemerythrin-like domain protein DcrH, CHLORO DIIRON-OXO MOIETY, CALCIUM ION, ... (4 entities in total)
Functional Keywords	metal-binding, helix bundle, oxygen sensor, metal binding protein
Biological source	Desulfovibrio vulgaris
Total number of polymer chains	2
Total formula weight	32772.98
Authors	Okamoto, Y.,Onoda, A.,Sugimoto, H.,Takano, Y.,Hirota, S.,Kurtz Jr., D.M.,Shiro, Y.,Hayashi, T. (deposition date: 2013-08-29, release date: 2014-02-26, Last modification date: 2023-11-08)
Primary citation	Okamoto, Y.,Onoda, A.,Sugimoto, H.,Takano, Y.,Hirota, S.,Kurtz Jr., D.M.,Shiro, Y.,Hayashi, T. H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin. Chem.Commun.(Camb.), 50:3421-3423, 2014 Cited by PubMed Abstract: The O2-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H2O2-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H2O2. PubMed: 24400317 DOI: 10.1039/c3cc48108e PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation