CROSS-LINKED HUMAN HEMOGLOBIN DEOXY
The structure was published by Bucci, E., Razynska, A., Kwansa, H., et al., Moult, J., Ji, X., and Gilliland, G., in 1996 in a paper entitled "Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1995.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN.
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: