1ydz Summary

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T-To-T(High) quaternary transitions in human hemoglobin: alphaY140F 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 3.3 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 (2-140) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
C Hemoglobin alpha chain P69905 (2-140) (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 - 140) 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) heme bindingsearch iron ion bindingsearch oxygen bindingsearch protein bindingsearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch peroxidase activitysearch oxygen transportsearch positive regulation of cell deathsearch transportsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch bicarbonate transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch receptor-mediated endocytosissearch response to hydrogen peroxidesearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch membranesearch
B, D (P68871) heme bindingsearch iron ion bindingsearch protein bindingsearch oxygen transporter activitysearch oxygen bindingsearch hemoglobin bindingsearch metal ion bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch transportsearch hydrogen peroxide catabolic processsearch nitric oxide transportsearch blood coagulationsearch bicarbonate transportsearch oxidation-reduction processsearch platelet aggregationsearch renal absorptionsearch positive regulation of cell deathsearch small molecule metabolic processsearch receptor-mediated endocytosissearch protein heterooligomerizationsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood pressuresearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch cytosolsearch extracellular vesicular exosomesearch extracellular regionsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch blood microparticlesearch endocytic vesicle lumensearch

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