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