REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION
The structure was published by Waller, D.A. and Liddington, R.C., in 1990 in a paper entitled "Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1990.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A (OXY) (ALPHA CHAIN) and HEMOGLOBIN A (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: