1xy0 Summary

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T-to-THigh Transitions in Human Hemoglobin: alphaK40G deoxy low-salt

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