Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom
The structure was published by Abdulmalik, O., Safo, M.K., Lerner, N.B., et al., Santacroce, R., Abraham, D.J., and Asakura, T., in 2004 in a paper entitled "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant with very low oxygen affinity" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 2003.
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: