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

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