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

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