1ye1 Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaY35A oxy (2MM IHP, 20% PEG) (1 test set)

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 4.5 Å and deposited in 2004.

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) Sequence family (Pfam)
A, C (P69905) Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch PF00042: Globinsearch

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

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