THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN
The structure was published by Smith, F.R., Lattman, E.E., and Carter Jr., C.W., in 1991 in a paper entitled "The mutation beta 99 Asp-Tyr stabilizes Y--a new, composite quaternary state of human hemoglobin." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 1992.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN YPSILANTI (CARBONMONOXY) (ALPHA CHAIN) and HEMOGLOBIN YPSILANTI (CARBONMONOXY) (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: