X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin. Compounds Designed to Link Primary and Secondary Binding Sites
The structure was published by Safo, M.K., Boyiri, T., Burnett, J.C., et al., Moure, C.M., Joshi, G.S., and Abraham, D.J., in 2002 in a paper entitled "X-ray crystallographic analyses of symmetrical allosteric effectors of hemoglobin: compounds designed to link primary and secondary binding sites." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.87 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely hemoglobin alpha chain and 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: