1ye2 Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaY35F oxy (2MM IHP, 20% PEG) (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 1.8 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 Cellular component (GO) Molecular function (GO) Biological process (GO)
A, C (P69905) hemoglobin complexsearch extracellular regionsearch cytosolsearch blood microparticlesearch endocytic vesicle lumensearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch membranesearch cytosolic small ribosomal subunitsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch heme bindingsearch peroxidase activitysearch metal ion bindingsearch haptoglobin bindingsearch oxygen transportsearch transportsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch response to hydrogen peroxidesearch small molecule metabolic processsearch protein heterooligomerizationsearch positive regulation of cell deathsearch receptor-mediated endocytosissearch oxidation-reduction processsearch
B, D (P68871) cytosolsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch hemoglobin complexsearch extracellular vesicular exosomesearch extracellular regionsearch blood microparticlesearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch hemoglobin bindingsearch metal ion bindingsearch oxygen transporter activitysearch heme bindingsearch oxygen transportsearch response to hydrogen peroxidesearch oxidation-reduction processsearch transportsearch small molecule metabolic processsearch regulation of blood pressuresearch blood coagulationsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch regulation of blood vessel sizesearch receptor-mediated endocytosissearch bicarbonate transportsearch renal absorptionsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch nitric oxide transportsearch protein heterooligomerizationsearch

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