1ygd Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaW37E alpha zinc beta oxy (10 TEST SETS)

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 2.73 Å and deposited in 2005.

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

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