1yhr Summary

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T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (10.0MM IHP, 20% PEG) (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 2.6 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) iron ion bindingsearch heme bindingsearch oxygen bindingsearch protein bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch metal ion bindingsearch peroxidase activitysearch hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch blood microparticlesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch membranesearch oxygen transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch bicarbonate transportsearch oxidation-reduction processsearch transportsearch protein heterooligomerizationsearch
B, D (P68871) iron ion bindingsearch heme bindingsearch oxygen bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch protein bindingsearch hemoglobin bindingsearch haptoglobin bindingsearch hemoglobin complexsearch extracellular regionsearch blood microparticlesearch extracellular vesicular exosomesearch cytosolsearch haptoglobin-hemoglobin complexsearch endocytic vesicle lumensearch oxygen transportsearch platelet aggregationsearch hydrogen peroxide catabolic processsearch bicarbonate transportsearch renal absorptionsearch positive regulation of nitric oxide biosynthetic processsearch small molecule metabolic processsearch protein heterooligomerizationsearch positive regulation of cell deathsearch oxidation-reduction processsearch blood coagulationsearch transportsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch regulation of blood pressuresearch nitric oxide transportsearch

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