1yh9 Summary

pdbe.org/1yh9
spacer

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