OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
The structure was published by Fronticelli, C., Pechik, I., Brinigar, W.S., Kowalczyk, J., and Gilliland, G.L., in 1994 in a paper entitled "Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted)." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN (DEOXY) (ALPHA CHAIN) and HEMOGLOBIN (DEOXY) (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: