Crystalline Human Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral pH In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure
The structure was published by Patskovska, L.N., Patskovsky, Y.V., Almo, S.C., and Hirsch, R.E., in 2005 in a paper entitled "COHbC and COHbS crystallize in the R2 quaternary state at neutral pH in the presence of PEG 4000." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2002.
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: