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

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