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

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