HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
The structure was published by Kavanaugh, J.S., Rogers, P.H., and Arnone, A., in 1992 in a paper entitled "High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from beta-globins having mutated amino termini." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1992.
The experimental data on which the structure is based was also 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: