1yeq Summary

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T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y 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 2.75 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) heme bindingsearch iron ion bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch oxygen bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch positive regulation of cell deathsearch hydrogen peroxide catabolic processsearch transportsearch bicarbonate transportsearch protein heterooligomerizationsearch small molecule metabolic processsearch response to hydrogen peroxidesearch oxidation-reduction processsearch cytosolsearch hemoglobin complexsearch blood microparticlesearch extracellular regionsearch endocytic vesicle lumensearch extracellular vesicular exosomesearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch membranesearch
B, D (P68871) heme bindingsearch oxygen bindingsearch iron ion bindingsearch metal ion bindingsearch protein bindingsearch oxygen transporter activitysearch haptoglobin bindingsearch hemoglobin bindingsearch peroxidase activitysearch oxygen transportsearch nitric oxide transportsearch positive regulation of nitric oxide biosynthetic processsearch regulation of blood vessel sizesearch protein heterooligomerizationsearch blood coagulationsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch renal absorptionsearch platelet aggregationsearch bicarbonate transportsearch transportsearch response to hydrogen peroxidesearch oxidation-reduction processsearch small molecule metabolic processsearch regulation of blood pressuresearch cytosolsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch blood microparticlesearch extracellular vesicular exosomesearch extracellular regionsearch 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