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

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