1yeu Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaW37G 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 2.12 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) oxygen bindingsearch heme bindingsearch iron ion bindingsearch protein bindingsearch peroxidase activitysearch metal ion bindingsearch haptoglobin bindingsearch oxygen transporter activitysearch oxygen transportsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch bicarbonate transportsearch transportsearch hydrogen peroxide catabolic processsearch small molecule metabolic processsearch positive regulation of cell deathsearch oxidation-reduction processsearch haptoglobin-hemoglobin complexsearch extracellular regionsearch hemoglobin complexsearch extracellular vesicular exosomesearch cytosolsearch endocytic vesicle lumensearch membranesearch cytosolic small ribosomal subunitsearch blood microparticlesearch
B, D (P68871) oxygen bindingsearch heme bindingsearch iron ion bindingsearch hemoglobin bindingsearch oxygen transporter activitysearch protein bindingsearch metal ion bindingsearch haptoglobin bindingsearch peroxidase activitysearch oxygen transportsearch protein heterooligomerizationsearch positive regulation of cell deathsearch bicarbonate transportsearch nitric oxide transportsearch renal absorptionsearch hydrogen peroxide catabolic processsearch response to hydrogen peroxidesearch regulation of blood pressuresearch platelet aggregationsearch regulation of blood vessel sizesearch transportsearch positive regulation of nitric oxide biosynthetic processsearch oxidation-reduction processsearch blood coagulationsearch small molecule metabolic processsearch hemoglobin complexsearch cytosolsearch blood microparticlesearch extracellular vesicular exosomesearch extracellular regionsearch 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