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

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