1y83 Summary

pdbe.org/1y83
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T-To-T(High) quaternary transitions in human hemoglobin: betaY145G deoxy low-salt (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 1.9 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 (2-145) (HBB_HUMAN)search Homo sapienssearch 98% 146 100%
D Hemoglobin beta chain P68871 (2-145) (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 - 145) 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 transporter activitysearch metal ion bindingsearch peroxidase activitysearch haptoglobin bindingsearch heme bindingsearch oxygen bindingsearch bicarbonate transportsearch oxygen transportsearch transportsearch positive regulation of cell deathsearch protein heterooligomerizationsearch small molecule metabolic processsearch oxidation-reduction processsearch response to hydrogen peroxidesearch hydrogen peroxide catabolic processsearch extracellular regionsearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch blood microparticlesearch endocytic vesicle lumensearch membranesearch cytosolic small ribosomal subunitsearch haptoglobin-hemoglobin complexsearch
B, D (P68871) oxygen bindingsearch protein bindingsearch oxygen transporter activitysearch iron ion bindingsearch peroxidase activitysearch hemoglobin bindingsearch metal ion bindingsearch haptoglobin bindingsearch heme bindingsearch blood coagulationsearch regulation of blood pressuresearch bicarbonate transportsearch positive regulation of nitric oxide biosynthetic processsearch platelet aggregationsearch oxidation-reduction processsearch renal absorptionsearch response to hydrogen peroxidesearch nitric oxide transportsearch transportsearch oxygen transportsearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch regulation of blood vessel sizesearch small molecule metabolic processsearch positive regulation of cell deathsearch hemoglobin complexsearch extracellular regionsearch cytosolsearch endocytic vesicle lumensearch haptoglobin-hemoglobin complexsearch extracellular vesicular exosomesearch 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