1hco Summary

pdbe.org/1hco
spacer

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