1y7z Summary

pdbe.org/1y7z
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T-To-T(High) quaternary transitions in human hemoglobin: betaN108A deoxy low-salt (1 test set)

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

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