1yeo Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaW37A OXY (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 2.22 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) Structural classification (CATH) Sequence family (Pfam)
A, C (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B, D (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

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