1yhe Summary

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T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (5.0MM 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 2.1 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) Cellular component (GO) Molecular function (GO)
A, C (P69905) oxygen transportsearch transportsearch bicarbonate transportsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch protein heterooligomerizationsearch small molecule metabolic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch membranesearch hemoglobin complexsearch extracellular regionsearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch blood microparticlesearch cytosolsearch protein bindingsearch haptoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch heme bindingsearch oxygen bindingsearch oxygen transporter activitysearch metal ion bindingsearch
B, D (P68871) protein heterooligomerizationsearch oxygen transportsearch regulation of blood vessel sizesearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch oxidation-reduction processsearch platelet aggregationsearch regulation of blood pressuresearch bicarbonate transportsearch small molecule metabolic processsearch renal absorptionsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch transportsearch blood coagulationsearch hemoglobin complexsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch cytosolsearch blood microparticlesearch endocytic vesicle lumensearch heme bindingsearch protein bindingsearch oxygen bindingsearch iron ion bindingsearch haptoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch hemoglobin bindingsearch peroxidase activitysearch

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