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

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