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