Dimeric horse myoglobin
The structure was published by Nagao, S., Osuka, H., Yamada, T., et al., Imai, K., Higuchi, Y., and Hirota, S., in 2012 in a paper entitled "Structural and oxygen binding properties of dimeric horse myoglobin" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.05 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Myoglobin.
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 most likely forms homodimers.
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: