1yh9 Summary

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T-to-T(High) quaternary transitions in human hemoglobin: HbA OXY (2MM 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 2.2 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) oxygen bindingsearch protein bindingsearch heme bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch peroxidase activitysearch iron ion bindingsearch metal ion bindingsearch extracellular regionsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch hemoglobin complexsearch blood microparticlesearch cytosolsearch membranesearch endocytic vesicle lumensearch cytosolic small ribosomal subunitsearch oxygen transportsearch bicarbonate transportsearch positive regulation of cell deathsearch protein heterooligomerizationsearch oxidation-reduction processsearch response to hydrogen peroxidesearch small molecule metabolic processsearch transportsearch hydrogen peroxide catabolic processsearch
B, D (P68871) protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch iron ion bindingsearch oxygen bindingsearch heme bindingsearch peroxidase activitysearch hemoglobin bindingsearch metal ion bindingsearch extracellular regionsearch cytosolsearch hemoglobin complexsearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch endocytic vesicle lumensearch oxygen transportsearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch nitric oxide transportsearch regulation of blood pressuresearch transportsearch positive regulation of cell deathsearch renal absorptionsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch regulation of blood vessel sizesearch platelet aggregationsearch response to hydrogen peroxidesearch blood coagulationsearch protein heterooligomerizationsearch 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