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

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