D136N mutant of Heme Oxygenase from Corynebacterium diphtheriae (HmuO)
The structure was published by Matsui, T., Furukawa, M., Unno, M., Tomita, T., and Ikeda-Saito, M., in 2005 in a paper entitled "Roles of Distal Asp in Heme Oxygenase from Corynebacterium diphtheriae, HmuO: A WATER-DRIVEN OXYGEN ACTIVATION MECHANISM" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Heme oxygenase.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: