1yzi Summary

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A novel quaternary structure of human carbonmonoxy hemoglobin

The structure was published by Safo, M.K. and Abraham, D.J., in 2005 in a paper entitled "The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbonmonoxy hemoglobin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.07 Å and deposited in 2005.

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%
B 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 (P69905) Globinssearch Globinssearch PF00042: Globinsearch
B (P68871) Globinssearch Globinssearch PF00042: Globinsearch

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

Chain InterPro annotation
A Globinsearch Haemoglobin, alphasearch Haemoglobin, pisearch Globin-likesearch Globin, structural domainsearch
B Globinsearch Haemoglobin, betasearch Globin-likesearch Globin, structural domainsearch