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

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