HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)
The structure was published by Kavanaugh, J.S., Moo-Penn, W.F., and Arnone, A., in 1993 in a paper entitled "Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1998.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely PROTEIN (HEMOGLOBIN ALPHA CHAIN) and PROTEIN (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: