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

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