1y0d Summary

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PDB entry 1y0d (supersedes 1dsh)

T-to-THigh Quaternary Transitions in Human Hemoglobin: desArg141alpha deoxy low-salt

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 2.1 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 (2-141) (HBA_HUMAN)search Homo sapienssearch 98% 140 100%
C Hemoglobin alpha chain P69905 (2-141) (HBA_HUMAN)search Homo sapienssearch 98% 140 100%
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 - 141) 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 oxygen transporter activitysearch haptoglobin bindingsearch metal ion bindingsearch peroxidase activitysearch oxygen transportsearch small molecule metabolic processsearch bicarbonate transportsearch response to hydrogen peroxidesearch transportsearch hydrogen peroxide catabolic processsearch positive regulation of cell deathsearch oxidation-reduction processsearch protein heterooligomerizationsearch hemoglobin complexsearch membranesearch endocytic vesicle lumensearch extracellular regionsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch cytosolic small ribosomal subunitsearch blood microparticlesearch cytosolsearch
B, D (P68871) iron ion bindingsearch metal ion bindingsearch protein bindingsearch heme bindingsearch oxygen transporter activitysearch peroxidase activitysearch haptoglobin bindingsearch oxygen bindingsearch hemoglobin bindingsearch oxygen transportsearch transportsearch oxidation-reduction processsearch protein heterooligomerizationsearch renal absorptionsearch regulation of blood pressuresearch blood coagulationsearch bicarbonate transportsearch nitric oxide transportsearch positive regulation of cell deathsearch small molecule metabolic processsearch hydrogen peroxide catabolic processsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch regulation of blood vessel sizesearch response to hydrogen peroxidesearch hemoglobin complexsearch cytosolsearch extracellular regionsearch extracellular vesicular exosomesearch blood microparticlesearch haptoglobin-hemoglobin complexsearch 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