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

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