1y0w Summary

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T-to-THigh quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (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 2.14 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 Biological process (GO) Cellular component (GO) Molecular function (GO)
A, C (P69905) hydrogen peroxide catabolic processsearch protein heterooligomerizationsearch oxidation-reduction processsearch transportsearch bicarbonate transportsearch response to hydrogen peroxidesearch oxygen transportsearch small molecule metabolic processsearch positive regulation of cell deathsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch cytosolsearch membranesearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch protein bindingsearch oxygen bindingsearch heme bindingsearch peroxidase activitysearch oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch iron ion bindingsearch
B, D (P68871) renal absorptionsearch oxygen transportsearch bicarbonate transportsearch regulation of blood pressuresearch nitric oxide transportsearch blood coagulationsearch small molecule metabolic processsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch transportsearch positive regulation of nitric oxide biosynthetic processsearch positive regulation of cell deathsearch platelet aggregationsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch hemoglobin complexsearch extracellular regionsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch cytosolsearch blood microparticlesearch endocytic vesicle lumensearch protein bindingsearch hemoglobin bindingsearch oxygen bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch iron ion bindingsearch heme bindingsearch

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