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

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