1y8w Summary

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T-To-T(High) quaternary transitions in human hemoglobin: alphaR92A oxy (2mM 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 2.9 Å and deposited in 2004.

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

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