1hho Summary

pdbe.org/1hho
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STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 ANGSTROMS RESOLUTION

The structure was published by Shaanan, B., in 1983 in a paper entitled "Structure of human oxyhaemoglobin at 2.1 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1983.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely HEMOGLOBIN A (OXY) (ALPHA CHAIN) and HEMOGLOBIN A (OXY) (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 A (OXY) (ALPHA CHAIN) P69905 (2-142) (HBA_HUMAN)search Homo sapienssearch 98% 141 100%
B HEMOGLOBIN A (OXY) (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 A (OXY) (ALPHA CHAIN) Homo sapiens
P68871 (2 - 147) HEMOGLOBIN A (OXY) (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 Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P69905) heme bindingsearch oxygen bindingsearch protein bindingsearch peroxidase activitysearch haptoglobin bindingsearch oxygen transporter activitysearch iron ion bindingsearch metal ion bindingsearch extracellular regionsearch hemoglobin complexsearch cytosolsearch extracellular vesicular exosomesearch blood microparticlesearch cytosolic small ribosomal subunitsearch endocytic vesicle lumensearch membranesearch haptoglobin-hemoglobin complexsearch oxygen transportsearch bicarbonate transportsearch positive regulation of cell deathsearch response to hydrogen peroxidesearch protein heterooligomerizationsearch hydrogen peroxide catabolic processsearch oxidation-reduction processsearch transportsearch small molecule metabolic processsearch receptor-mediated endocytosissearch
B (P68871) heme bindingsearch protein bindingsearch oxygen bindingsearch haptoglobin bindingsearch hemoglobin bindingsearch iron ion bindingsearch peroxidase activitysearch oxygen transporter activitysearch metal ion bindingsearch extracellular regionsearch endocytic vesicle lumensearch cytosolsearch hemoglobin complexsearch extracellular vesicular exosomesearch haptoglobin-hemoglobin complexsearch blood microparticlesearch positive regulation of nitric oxide biosynthetic processsearch response to hydrogen peroxidesearch bicarbonate transportsearch platelet aggregationsearch small molecule metabolic processsearch protein heterooligomerizationsearch receptor-mediated endocytosissearch oxygen transportsearch oxidation-reduction processsearch blood coagulationsearch transportsearch nitric oxide transportsearch regulation of blood pressuresearch regulation of blood vessel sizesearch hydrogen peroxide catabolic processsearch renal absorptionsearch positive regulation of cell deathsearch

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