1yhr Summary

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T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (10.0MM IHP, 20% PEG) (10 test sets)

The structure was published by Kavanaugh, J.S., Rogers, P.H., and Arnone, A., in 2005 in a paper entitled "Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2005.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain P68871 (2-147) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P69905 (2 - 142) Hemoglobin alpha chain Homo sapiens
P68871 (2 - 147) Hemoglobin beta chain Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, C (P69905) oxygen transportsearch transportsearch receptor-mediated endocytosissearch oxidation-reduction processsearch bicarbonate transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch protein bindingsearch oxygen transporter activitysearch metal ion bindingsearch peroxidase activitysearch heme bindingsearch oxygen bindingsearch iron ion bindingsearch haptoglobin bindingsearch membranesearch extracellular vesicular exosomesearch hemoglobin complexsearch extracellular regionsearch cytosolsearch blood microparticlesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch
B, D (P68871) regulation of blood vessel sizesearch blood coagulationsearch oxygen transportsearch oxidation-reduction processsearch nitric oxide transportsearch transportsearch renal absorptionsearch response to hydrogen peroxidesearch bicarbonate transportsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch regulation of blood pressuresearch protein heterooligomerizationsearch small molecule metabolic processsearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch receptor-mediated endocytosissearch oxygen bindingsearch oxygen transporter activitysearch protein bindingsearch iron ion bindingsearch heme bindingsearch peroxidase activitysearch hemoglobin bindingsearch metal ion bindingsearch haptoglobin bindingsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch hemoglobin complexsearch cytosolsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch blood microparticlesearch

Chain InterPro annotation
A, C Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B, D Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch