1y31 Summary

pdbe.org/1y31
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T-To-T(High) quaternary transitions in human hemoglobin: betaY35A 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 2.13 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) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch metal ion bindingsearch oxygen transportsearch protein heterooligomerizationsearch response to hydrogen peroxidesearch transportsearch receptor-mediated endocytosissearch small molecule metabolic processsearch bicarbonate transportsearch positive regulation of cell deathsearch oxidation-reduction processsearch hydrogen peroxide catabolic processsearch hemoglobin complexsearch extracellular regionsearch membranesearch cytosolic small ribosomal subunitsearch blood microparticlesearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch cytosolsearch extracellular exosomesearch
B, D (P68871) iron ion bindingsearch heme bindingsearch protein bindingsearch oxygen bindingsearch oxygen transporter activitysearch metal ion bindingsearch haptoglobin bindingsearch peroxidase activitysearch hemoglobin bindingsearch oxygen transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch bicarbonate transportsearch regulation of blood vessel sizesearch hydrogen peroxide catabolic processsearch renal absorptionsearch small molecule metabolic processsearch nitric oxide transportsearch platelet aggregationsearch transportsearch regulation of blood pressuresearch protein heterooligomerizationsearch oxidation-reduction processsearch receptor-mediated endocytosissearch positive regulation of nitric oxide biosynthetic processsearch blood coagulationsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch cytosolsearch extracellular regionsearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular exosomesearch

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