1HDA

A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN

Summary for 1HDA

Entry DOI	10.2210/pdb1hda/pdb
Descriptor	HEMOGLOBIN (DEOXY) (ALPHA CHAIN), HEMOGLOBIN (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
Functional Keywords	oxygen transport
Biological source	Bos taurus (cattle) More
Total number of polymer chains	4
Total formula weight	64575.05
Authors	Fermi, G. (deposition date: 1993-05-06, release date: 1994-05-31, Last modification date: 2024-02-07)
Primary citation	Perutz, M.F.,Fermi, G.,Poyart, C.,Pagnier, J.,Kister, J. A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J.Mol.Biol., 233:536-545, 1993 Cited by PubMed: 8411160 DOI: 10.1006/jmbi.1993.1530 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation