MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
The structure was published by Miyazaki, G., Morimoto, H., Yun, K.M., et al., Nakagawa, A., Minagawa, H., and Shibayama, N., in 1999 in a paper entitled "Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely PROTEIN (HEMOGLOBIN ALPHA CHAIN) and PROTEIN (HEMOGLOBIN BETA CHAIN).
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 heterotetramers.
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 2 unique UniProt proteins: