1hco Summary

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THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION

The structure was published by Baldwin, J.M., in 1980 in a paper entitled "The structure of human carbonmonoxy haemoglobin at 2.7 A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 1979.

The experimental data on which the structure is based was not deposited.

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